ATOM 1 N THR A 3 -28.938 29.195 29.551 1.00 75.39 N1+ ANISOU 1 N THR A 3 11265 10585 6796 640 -566 -146 N1+ ATOM 2 CA THR A 3 -27.718 28.449 29.086 1.00 75.90 C ANISOU 2 CA THR A 3 11324 10776 6737 857 -712 -92 C ATOM 3 C THR A 3 -28.178 27.162 28.355 1.00 75.91 C ANISOU 3 C THR A 3 11536 10589 6718 977 -633 69 C ATOM 4 O THR A 3 -27.579 26.838 27.331 1.00 74.23 O ANISOU 4 O THR A 3 11268 10386 6552 1090 -692 114 O ATOM 5 CB THR A 3 -26.692 28.094 30.200 1.00 77.44 C ANISOU 5 CB THR A 3 11574 11188 6662 1004 -852 -135 C ATOM 6 CG2 THR A 3 -26.053 29.336 30.840 1.00 76.98 C ANISOU 6 CG2 THR A 3 11283 11335 6630 870 -950 -321 C ATOM 7 OG1 THR A 3 -27.288 27.332 31.236 1.00 78.83 O ANISOU 7 OG1 THR A 3 12019 11259 6674 1021 -752 -74 O ATOM 8 N ASN A 4 -29.291 26.516 28.745 1.00 76.47 N ANISOU 8 N ASN A 4 11853 10481 6719 946 -489 152 N ATOM 9 CA ASN A 4 -29.922 25.417 27.992 1.00 77.68 C ANISOU 9 CA ASN A 4 12224 10418 6872 1006 -384 294 C ATOM 10 C ASN A 4 -30.234 25.794 26.529 1.00 74.64 C ANISOU 10 C ASN A 4 11711 9902 6745 866 -307 291 C ATOM 11 O ASN A 4 -29.986 24.989 25.638 1.00 74.54 O ANISOU 11 O ASN A 4 11822 9745 6754 927 -264 379 O ATOM 12 CB ASN A 4 -31.227 24.941 28.675 1.00 79.91 C ANISOU 12 CB ASN A 4 12776 10543 7043 945 -217 369 C ATOM 13 CG ASN A 4 -31.024 24.364 30.075 1.00 85.70 C ANISOU 13 CG ASN A 4 13724 11367 7471 1140 -284 423 C ATOM 14 ND2 ASN A 4 -31.002 23.044 30.211 1.00 87.24 N ANISOU 14 ND2 ASN A 4 13787 11812 7550 1290 -485 354 N ATOM 15 OD1 ASN A 4 -30.899 25.110 31.041 1.00 87.75 O ANISOU 15 OD1 ASN A 4 14265 11484 7592 1152 -154 528 O ATOM 16 N PHE A 5 -30.712 27.026 26.297 1.00 70.74 N ANISOU 16 N PHE A 5 10986 9453 6437 686 -289 191 N ATOM 17 CA PHE A 5 -31.145 27.514 24.978 1.00 65.20 C ANISOU 17 CA PHE A 5 10148 8656 5969 555 -225 184 C ATOM 18 C PHE A 5 -29.992 27.666 23.957 1.00 64.67 C ANISOU 18 C PHE A 5 9890 8705 5977 630 -353 154 C ATOM 19 O PHE A 5 -30.238 27.586 22.757 1.00 66.49 O ANISOU 19 O PHE A 5 10112 8847 6305 633 -327 196 O ATOM 20 CB PHE A 5 -31.930 28.833 25.180 1.00 58.43 C ANISOU 20 CB PHE A 5 9154 7787 5261 355 -139 104 C ATOM 21 CG PHE A 5 -32.753 29.370 24.014 1.00 56.78 C ANISOU 21 CG PHE A 5 8807 7494 5273 230 -74 103 C ATOM 22 CD1 PHE A 5 -33.536 28.505 23.214 1.00 59.38 C ANISOU 22 CD1 PHE A 5 9235 7665 5660 158 53 166 C ATOM 23 CD2 PHE A 5 -32.922 30.765 23.861 1.00 55.72 C ANISOU 23 CD2 PHE A 5 8446 7445 5280 176 -137 37 C ATOM 24 CE1 PHE A 5 -34.389 29.022 22.249 1.00 57.22 C ANISOU 24 CE1 PHE A 5 8822 7346 5575 51 96 157 C ATOM 25 CE2 PHE A 5 -33.791 31.261 22.898 1.00 55.83 C ANISOU 25 CE2 PHE A 5 8344 7394 5476 82 -84 47 C ATOM 26 CZ PHE A 5 -34.509 30.394 22.089 1.00 56.72 C ANISOU 26 CZ PHE A 5 8541 7373 5636 27 23 103 C ATOM 27 N SER A 6 -28.751 27.825 24.440 1.00 63.07 N ANISOU 27 N SER A 6 9529 8710 5726 679 -486 73 N ATOM 28 CA SER A 6 -27.549 27.877 23.603 1.00 66.34 C ANISOU 28 CA SER A 6 9743 9264 6199 746 -598 40 C ATOM 29 C SER A 6 -26.856 26.500 23.491 1.00 67.41 C ANISOU 29 C SER A 6 9982 9435 6196 992 -678 111 C ATOM 30 O SER A 6 -25.791 26.427 22.879 1.00 66.94 O ANISOU 30 O SER A 6 9796 9441 6198 1061 -730 107 O ATOM 31 CB SER A 6 -26.583 28.944 24.173 1.00 73.70 C ANISOU 31 CB SER A 6 10465 10418 7119 696 -705 -82 C ATOM 32 OG SER A 6 -27.051 30.260 23.916 1.00 78.95 O ANISOU 32 OG SER A 6 11076 11023 7897 489 -623 -150 O ATOM 33 N THR A 7 -27.432 25.440 24.079 1.00 71.40 N ANISOU 33 N THR A 7 10724 9896 6507 1138 -681 181 N ATOM 34 CA THR A 7 -26.847 24.100 24.090 1.00 73.94 C ANISOU 34 CA THR A 7 11191 10220 6684 1405 -746 264 C ATOM 35 C THR A 7 -27.730 23.141 23.248 1.00 75.59 C ANISOU 35 C THR A 7 11592 10159 6969 1394 -618 355 C ATOM 36 O THR A 7 -28.894 22.951 23.606 1.00 72.26 O ANISOU 36 O THR A 7 11386 9531 6540 1293 -483 416 O ATOM 37 CB THR A 7 -26.807 23.561 25.546 1.00 77.88 C ANISOU 37 CB THR A 7 11900 10765 6926 1579 -796 317 C ATOM 38 CG2 THR A 7 -26.086 22.209 25.693 1.00 79.23 C ANISOU 38 CG2 THR A 7 12265 10898 6943 1885 -848 425 C ATOM 39 OG1 THR A 7 -26.127 24.485 26.383 1.00 77.49 O ANISOU 39 OG1 THR A 7 11653 11001 6790 1595 -938 210 O ATOM 40 N PRO A 8 -27.206 22.573 22.136 1.00 78.50 N ANISOU 40 N PRO A 8 11888 10529 7410 1482 -649 357 N ATOM 41 CA PRO A 8 -27.959 21.570 21.353 1.00 82.05 C ANISOU 41 CA PRO A 8 12532 10720 7925 1462 -532 423 C ATOM 42 C PRO A 8 -28.128 20.233 22.106 1.00 89.09 C ANISOU 42 C PRO A 8 13778 11443 8630 1658 -497 537 C ATOM 43 O PRO A 8 -27.317 19.912 22.976 1.00 92.79 O ANISOU 43 O PRO A 8 14306 12032 8917 1917 -607 571 O ATOM 44 CB PRO A 8 -27.122 21.422 20.073 1.00 81.07 C ANISOU 44 CB PRO A 8 12228 10687 7888 1544 -596 380 C ATOM 45 CG PRO A 8 -25.700 21.739 20.501 1.00 80.85 C ANISOU 45 CG PRO A 8 12006 10953 7761 1721 -756 333 C ATOM 46 CD PRO A 8 -25.874 22.808 21.572 1.00 80.56 C ANISOU 46 CD PRO A 8 11886 11035 7689 1597 -785 288 C ATOM 47 N LEU A 9 -29.185 19.477 21.772 1.00 94.45 N ANISOU 47 N LEU A 9 14693 11843 9350 1533 -340 595 N ATOM 48 CA LEU A 9 -29.449 18.160 22.352 1.00102.53 C ANISOU 48 CA LEU A 9 16101 12652 10206 1675 -267 715 C ATOM 49 C LEU A 9 -28.387 17.133 21.919 1.00106.44 C ANISOU 49 C LEU A 9 16725 13069 10649 1931 -312 752 C ATOM 50 O LEU A 9 -28.378 16.718 20.759 1.00105.91 O ANISOU 50 O LEU A 9 16611 12910 10721 1857 -271 708 O ATOM 51 CB LEU A 9 -30.879 17.700 21.972 1.00105.80 C ANISOU 51 CB LEU A 9 16710 12798 10692 1415 -68 751 C ATOM 52 CG LEU A 9 -31.307 16.310 22.504 1.00109.03 C ANISOU 52 CG LEU A 9 17080 13257 11089 1227 0 741 C ATOM 53 CD1 LEU A 9 -31.201 16.224 24.037 1.00108.66 C ANISOU 53 CD1 LEU A 9 17166 12982 11138 952 205 759 C ATOM 54 CD2 LEU A 9 -32.714 15.933 22.001 1.00109.28 C ANISOU 54 CD2 LEU A 9 17301 13349 10871 1426 -47 821 C ATOM 55 N ASN A 10 -27.551 16.693 22.867 1.00104.46 N ANISOU 55 N ASN A 10 16639 12863 10186 2248 -397 830 N ATOM 56 CA ASN A 10 -26.570 15.632 22.643 1.00103.95 C ANISOU 56 CA ASN A 10 16711 12740 10044 2556 -447 872 C ATOM 57 C ASN A 10 -27.251 14.250 22.698 1.00102.64 C ANISOU 57 C ASN A 10 16986 12175 9838 2552 -277 975 C ATOM 58 O ASN A 10 -27.079 13.484 23.648 1.00106.21 O ANISOU 58 O ASN A 10 17764 12488 10101 2702 -237 1100 O ATOM 59 CB ASN A 10 -25.369 15.753 23.611 1.00108.45 C ANISOU 59 CB ASN A 10 17263 13547 10394 2918 -617 914 C ATOM 60 CG ASN A 10 -24.125 15.135 22.974 1.00113.42 C ANISOU 60 CG ASN A 10 18005 14150 10939 3284 -678 952 C ATOM 61 ND2 ASN A 10 -23.098 15.934 22.714 1.00114.76 N ANISOU 61 ND2 ASN A 10 17836 14631 11135 3432 -827 860 N ATOM 62 OD1 ASN A 10 -24.118 13.956 22.626 1.00116.40 O ANISOU 62 OD1 ASN A 10 18775 14228 11223 3433 -584 1061 O ATOM 63 N GLU A 11 -28.033 13.962 21.652 1.00 99.14 N ANISOU 63 N GLU A 11 16566 11543 9562 2375 -174 922 N ATOM 64 CA GLU A 11 -28.846 12.760 21.460 1.00100.69 C ANISOU 64 CA GLU A 11 17173 11345 9739 2317 1 995 C ATOM 65 C GLU A 11 -28.094 11.412 21.568 1.00105.11 C ANISOU 65 C GLU A 11 18034 11748 10155 2690 -21 1071 C ATOM 66 O GLU A 11 -28.743 10.389 21.762 1.00107.56 O ANISOU 66 O GLU A 11 18735 11697 10434 2667 130 1135 O ATOM 67 CB GLU A 11 -29.611 12.880 20.121 1.00 99.80 C ANISOU 67 CB GLU A 11 16972 11102 9846 1983 111 892 C ATOM 68 CG GLU A 11 -28.746 13.332 18.913 1.00101.10 C ANISOU 68 CG GLU A 11 16947 11355 10110 2072 32 790 C ATOM 69 CD GLU A 11 -29.435 13.193 17.550 1.00102.46 C ANISOU 69 CD GLU A 11 17047 11410 10473 1742 133 689 C ATOM 70 OE1 GLU A 11 -30.549 12.628 17.506 1.00101.49 O ANISOU 70 OE1 GLU A 11 16612 11465 10485 1499 115 618 O ATOM 71 OE2 GLU A 11 -28.799 13.601 16.555 1.00104.87 O1- ANISOU 71 OE2 GLU A 11 17618 11443 10785 1729 230 677 O1- ATOM 72 N TYR A 12 -26.759 11.426 21.456 1.00107.74 N ANISOU 72 N TYR A 12 18195 12341 10399 3031 -196 1059 N ATOM 73 CA TYR A 12 -25.893 10.251 21.586 1.00111.23 C ANISOU 73 CA TYR A 12 18928 12665 10670 3451 -229 1148 C ATOM 74 C TYR A 12 -25.695 9.816 23.046 1.00116.35 C ANISOU 74 C TYR A 12 19880 13253 11074 3675 -237 1311 C ATOM 75 O TYR A 12 -25.510 8.629 23.301 1.00122.24 O ANISOU 75 O TYR A 12 20990 13795 11663 4001 -215 1423 O ATOM 76 CB TYR A 12 -24.518 10.543 20.952 1.00111.14 C ANISOU 76 CB TYR A 12 18589 12992 10649 3749 -413 1070 C ATOM 77 CG TYR A 12 -24.539 10.827 19.461 1.00109.27 C ANISOU 77 CG TYR A 12 18158 12759 10600 3634 -390 936 C ATOM 78 CD1 TYR A 12 -24.904 12.105 18.993 1.00107.94 C ANISOU 78 CD1 TYR A 12 17586 12813 10616 3327 -419 814 C ATOM 79 CD2 TYR A 12 -24.170 9.824 18.538 1.00110.48 C ANISOU 79 CD2 TYR A 12 18551 12690 10735 3845 -333 934 C ATOM 80 CE1 TYR A 12 -24.902 12.379 17.614 1.00107.60 C ANISOU 80 CE1 TYR A 12 17377 12785 10721 3232 -399 701 C ATOM 81 CE2 TYR A 12 -24.152 10.105 17.158 1.00109.72 C ANISOU 81 CE2 TYR A 12 18286 12611 10791 3744 -311 805 C ATOM 82 CZ TYR A 12 -24.505 11.387 16.700 1.00109.14 C ANISOU 82 CZ TYR A 12 17805 12777 10887 3437 -346 693 C ATOM 83 OH TYR A 12 -24.455 11.679 15.374 1.00110.28 O ANISOU 83 OH TYR A 12 17791 12949 11160 3344 -325 573 O ATOM 84 N GLU A 13 -25.716 10.783 23.967 1.00115.59 N ANISOU 84 N GLU A 13 19661 13326 10933 3519 -265 1328 N ATOM 85 CA GLU A 13 -25.535 10.573 25.406 1.00119.98 C ANISOU 85 CA GLU A 13 20504 13845 11240 3704 -269 1480 C ATOM 86 C GLU A 13 -26.871 10.391 26.154 1.00118.77 C ANISOU 86 C GLU A 13 20613 13428 11087 3376 -66 1552 C ATOM 87 O GLU A 13 -26.846 9.947 27.302 1.00121.53 O ANISOU 87 O GLU A 13 21229 13666 11283 3478 -7 1659 O ATOM 88 CB GLU A 13 -24.745 11.769 25.979 1.00122.92 C ANISOU 88 CB GLU A 13 20536 14668 11499 3845 -481 1439 C ATOM 89 CG GLU A 13 -23.327 11.906 25.382 1.00128.38 C ANISOU 89 CG GLU A 13 21000 15633 12145 4227 -666 1383 C ATOM 90 CD GLU A 13 -22.543 13.123 25.882 1.00134.19 C ANISOU 90 CD GLU A 13 21536 16708 12741 4387 -820 1366 C ATOM 91 OE1 GLU A 13 -23.077 13.878 26.724 1.00134.30 O ANISOU 91 OE1 GLU A 13 21431 16866 12731 4168 -843 1342 O ATOM 92 OE2 GLU A 13 -21.405 13.289 25.390 1.00138.51 O1- ANISOU 92 OE2 GLU A 13 22054 17378 13195 4733 -914 1369 O1- ATOM 93 N GLU A 14 -28.000 10.728 25.506 1.00113.17 N ANISOU 93 N GLU A 14 19744 12650 10605 2951 52 1450 N ATOM 94 CA GLU A 14 -29.356 10.603 26.043 1.00112.75 C ANISOU 94 CA GLU A 14 19900 12375 10563 2626 256 1504 C ATOM 95 C GLU A 14 -29.789 9.144 26.253 1.00113.95 C ANISOU 95 C GLU A 14 20573 12075 10648 2642 452 1628 C ATOM 96 O GLU A 14 -29.653 8.330 25.339 1.00116.15 O ANISOU 96 O GLU A 14 20973 12164 10995 2726 477 1603 O ATOM 97 CB GLU A 14 -30.343 11.295 25.076 1.00111.87 C ANISOU 97 CB GLU A 14 19468 12320 10718 2195 326 1356 C ATOM 98 CG GLU A 14 -30.369 12.836 25.161 1.00112.47 C ANISOU 98 CG GLU A 14 19069 12793 10871 2135 167 1240 C ATOM 99 CD GLU A 14 -30.946 13.392 26.468 1.00115.07 C ANISOU 99 CD GLU A 14 19412 13291 11018 2192 124 1296 C ATOM 100 OE1 GLU A 14 -31.649 12.634 27.173 1.00117.30 O ANISOU 100 OE1 GLU A 14 19998 13380 11192 2098 281 1400 O ATOM 101 OE2 GLU A 14 -30.684 14.587 26.728 1.00114.70 O1- ANISOU 101 OE2 GLU A 14 19075 13574 10932 2320 -60 1231 O1- ATOM 102 N VAL A 15 -30.372 8.879 27.435 1.00113.26 N ANISOU 102 N VAL A 15 20807 11808 10420 2552 605 1758 N ATOM 103 CA VAL A 15 -31.031 7.617 27.788 1.00113.30 C ANISOU 103 CA VAL A 15 21229 11406 10415 2512 809 1824 C ATOM 104 C VAL A 15 -32.357 7.422 27.016 1.00111.87 C ANISOU 104 C VAL A 15 21158 10938 10411 2095 1017 1779 C ATOM 105 O VAL A 15 -32.716 6.285 26.709 1.00114.31 O ANISOU 105 O VAL A 15 21758 10912 10763 2062 1151 1779 O ATOM 106 CB VAL A 15 -31.301 7.541 29.321 1.00114.33 C ANISOU 106 CB VAL A 15 21554 11497 10390 2526 901 1922 C ATOM 107 CG1 VAL A 15 -32.155 6.338 29.781 1.00117.08 C ANISOU 107 CG1 VAL A 15 22344 11443 10697 2543 1095 1994 C ATOM 108 CG2 VAL A 15 -29.977 7.545 30.108 1.00114.33 C ANISOU 108 CG2 VAL A 15 21385 11834 10221 2898 676 1946 C ATOM 109 N SER A 16 -33.028 8.539 26.674 1.00108.92 N ANISOU 109 N SER A 16 20434 10746 10206 1743 1037 1664 N ATOM 110 CA SER A 16 -34.252 8.599 25.869 1.00108.81 C ANISOU 110 CA SER A 16 20384 10551 10409 1314 1214 1560 C ATOM 111 C SER A 16 -34.082 8.071 24.427 1.00104.56 C ANISOU 111 C SER A 16 19753 9942 10033 1320 1159 1434 C ATOM 112 O SER A 16 -35.069 7.637 23.833 1.00102.43 O ANISOU 112 O SER A 16 19544 9466 9910 1000 1309 1354 O ATOM 113 CB SER A 16 -34.752 10.061 25.879 1.00111.61 C ANISOU 113 CB SER A 16 20317 11177 10912 990 1218 1448 C ATOM 114 OG SER A 16 -35.988 10.220 25.209 1.00114.39 O ANISOU 114 OG SER A 16 20588 11404 11471 592 1367 1337 O ATOM 115 N TYR A 17 -32.848 8.126 23.897 1.00104.99 N ANISOU 115 N TYR A 17 19652 10179 10058 1666 951 1406 N ATOM 116 CA TYR A 17 -32.505 7.749 22.524 1.00106.59 C ANISOU 116 CA TYR A 17 19769 10342 10389 1715 894 1288 C ATOM 117 C TYR A 17 -31.392 6.680 22.488 1.00111.51 C ANISOU 117 C TYR A 17 20710 10810 10850 2161 836 1378 C ATOM 118 O TYR A 17 -30.792 6.475 21.434 1.00110.77 O ANISOU 118 O TYR A 17 20437 10861 10789 2394 692 1302 O ATOM 119 CB TYR A 17 -32.132 9.026 21.730 1.00104.26 C ANISOU 119 CB TYR A 17 18925 10446 10242 1689 708 1143 C ATOM 120 CG TYR A 17 -33.139 10.164 21.829 1.00105.71 C ANISOU 120 CG TYR A 17 18787 10842 10537 1363 727 1087 C ATOM 121 CD1 TYR A 17 -34.468 9.978 21.396 1.00107.57 C ANISOU 121 CD1 TYR A 17 18982 10959 10929 954 881 1011 C ATOM 122 CD2 TYR A 17 -32.762 11.403 22.388 1.00106.41 C ANISOU 122 CD2 TYR A 17 18609 11253 10570 1470 591 1101 C ATOM 123 CE1 TYR A 17 -35.416 11.010 21.541 1.00107.34 C ANISOU 123 CE1 TYR A 17 18656 11129 10998 691 901 960 C ATOM 124 CE2 TYR A 17 -33.711 12.430 22.551 1.00106.18 C ANISOU 124 CE2 TYR A 17 18308 11396 10641 1193 617 1045 C ATOM 125 CZ TYR A 17 -35.039 12.236 22.124 1.00106.80 C ANISOU 125 CZ TYR A 17 18353 11353 10874 819 774 980 C ATOM 126 OH TYR A 17 -35.955 13.236 22.267 1.00106.08 O ANISOU 126 OH TYR A 17 17987 11438 10879 576 803 925 O ATOM 127 N GLU A 18 -31.143 6.003 23.624 1.00117.30 N ANISOU 127 N GLU A 18 21926 11244 11397 2297 958 1547 N ATOM 128 CA GLU A 18 -30.109 4.976 23.805 1.00119.64 C ANISOU 128 CA GLU A 18 22526 11394 11539 2737 916 1628 C ATOM 129 C GLU A 18 -30.320 3.690 22.978 1.00120.04 C ANISOU 129 C GLU A 18 22887 11055 11666 2672 1064 1564 C ATOM 130 O GLU A 18 -29.336 3.010 22.685 1.00122.32 O ANISOU 130 O GLU A 18 23280 11303 11892 3024 1001 1550 O ATOM 131 CB GLU A 18 -29.975 4.705 25.321 1.00123.44 C ANISOU 131 CB GLU A 18 23205 11854 11842 2885 963 1742 C ATOM 132 CG GLU A 18 -28.999 3.586 25.748 1.00130.51 C ANISOU 132 CG GLU A 18 24286 12712 12590 3350 896 1784 C ATOM 133 CD GLU A 18 -28.878 3.413 27.267 1.00138.27 C ANISOU 133 CD GLU A 18 25509 13632 13394 3472 964 1904 C ATOM 134 OE1 GLU A 18 -29.468 4.227 28.012 1.00139.55 O ANISOU 134 OE1 GLU A 18 25569 13935 13519 3307 972 1952 O ATOM 135 OE2 GLU A 18 -28.187 2.449 27.661 1.00143.76 O1- ANISOU 135 OE2 GLU A 18 26507 14138 13979 3738 1013 1951 O1- ATOM 136 N SER A 19 -31.579 3.387 22.609 1.00113.88 N ANISOU 136 N SER A 19 22234 10014 11020 2221 1260 1509 N ATOM 137 CA SER A 19 -31.976 2.202 21.842 1.00112.76 C ANISOU 137 CA SER A 19 22397 9497 10948 2086 1422 1426 C ATOM 138 C SER A 19 -31.314 2.112 20.453 1.00105.08 C ANISOU 138 C SER A 19 21364 8530 10030 2326 1305 1322 C ATOM 139 O SER A 19 -30.974 3.139 19.863 1.00104.60 O ANISOU 139 O SER A 19 20881 8827 10035 2429 1115 1248 O ATOM 140 CB SER A 19 -33.518 2.153 21.762 1.00116.84 C ANISOU 140 CB SER A 19 22920 9843 11632 1516 1610 1340 C ATOM 141 OG SER A 19 -34.052 3.069 20.823 1.00116.84 O ANISOU 141 OG SER A 19 22435 10147 11813 1312 1493 1187 O ATOM 142 N ALA A 20 -31.164 0.870 19.959 1.00 97.13 N ANISOU 142 N ALA A 20 20673 7221 9010 2380 1416 1266 N ATOM 143 CA ALA A 20 -30.541 0.540 18.674 1.00 99.48 C ANISOU 143 CA ALA A 20 20935 7515 9346 2623 1324 1155 C ATOM 144 C ALA A 20 -31.234 1.156 17.444 1.00 93.48 C ANISOU 144 C ALA A 20 19874 6852 8792 2310 1286 979 C ATOM 145 O ALA A 20 -30.546 1.443 16.465 1.00 93.27 O ANISOU 145 O ALA A 20 19567 7061 8811 2503 1140 866 O ATOM 146 CB ALA A 20 -30.460 -0.987 18.537 1.00107.55 C ANISOU 146 CB ALA A 20 22368 8185 10311 2683 1477 1119 C ATOM 147 N GLY A 21 -32.559 1.379 17.528 1.00 87.71 N ANISOU 147 N GLY A 21 19063 6071 8191 1793 1409 910 N ATOM 148 CA GLY A 21 -33.363 2.000 16.476 1.00 82.02 C ANISOU 148 CA GLY A 21 17896 5604 7665 1463 1348 705 C ATOM 149 C GLY A 21 -33.047 3.496 16.339 1.00 75.13 C ANISOU 149 C GLY A 21 16455 5256 6835 1557 1135 693 C ATOM 150 O GLY A 21 -32.931 3.983 15.217 1.00 72.93 O ANISOU 150 O GLY A 21 15838 5229 6642 1597 1006 560 O ATOM 151 N TYR A 22 -32.861 4.211 17.464 1.00 77.98 N ANISOU 151 N TYR A 22 16720 5780 7128 1589 1103 828 N ATOM 152 CA TYR A 22 -32.409 5.605 17.474 1.00 79.14 C ANISOU 152 CA TYR A 22 16359 6401 7309 1671 910 814 C ATOM 153 C TYR A 22 -30.912 5.760 17.161 1.00 81.27 C ANISOU 153 C TYR A 22 16510 6878 7492 2141 728 825 C ATOM 154 O TYR A 22 -30.544 6.788 16.600 1.00 68.22 O ANISOU 154 O TYR A 22 14409 5604 5908 2179 572 751 O ATOM 155 CB TYR A 22 -32.760 6.270 18.820 1.00 80.84 C ANISOU 155 CB TYR A 22 16548 6720 7447 1620 924 948 C ATOM 156 CG TYR A 22 -34.154 6.863 18.896 1.00 83.00 C ANISOU 156 CG TYR A 22 16608 7066 7861 1152 1016 886 C ATOM 157 CD1 TYR A 22 -34.489 7.967 18.081 1.00 81.68 C ANISOU 157 CD1 TYR A 22 15948 7236 7850 981 907 760 C ATOM 158 CD2 TYR A 22 -35.108 6.346 19.795 1.00 86.09 C ANISOU 158 CD2 TYR A 22 17291 7196 8223 894 1219 959 C ATOM 159 CE1 TYR A 22 -35.771 8.543 18.160 1.00 83.51 C ANISOU 159 CE1 TYR A 22 15977 7547 8206 591 986 705 C ATOM 160 CE2 TYR A 22 -36.390 6.925 19.877 1.00 87.65 C ANISOU 160 CE2 TYR A 22 17266 7488 8547 482 1306 896 C ATOM 161 CZ TYR A 22 -36.721 8.024 19.060 1.00 87.60 C ANISOU 161 CZ TYR A 22 16762 7825 8695 346 1183 767 C ATOM 162 OH TYR A 22 -37.958 8.594 19.145 1.00 89.76 O ANISOU 162 OH TYR A 22 16808 8205 9091 -27 1266 705 O ATOM 163 N THR A 23 -30.082 4.759 17.506 1.00 85.26 N ANISOU 163 N THR A 23 17408 7142 7845 2504 754 918 N ATOM 164 CA THR A 23 -28.634 4.781 17.277 1.00 83.48 C ANISOU 164 CA THR A 23 17059 7135 7523 2980 584 931 C ATOM 165 C THR A 23 -28.266 4.765 15.780 1.00 83.99 C ANISOU 165 C THR A 23 16914 7296 7701 2992 534 756 C ATOM 166 O THR A 23 -27.419 5.562 15.375 1.00 81.91 O ANISOU 166 O THR A 23 16260 7409 7455 3170 372 701 O ATOM 167 CB THR A 23 -27.916 3.604 17.989 1.00 86.80 C ANISOU 167 CB THR A 23 17977 7264 7741 3393 631 1084 C ATOM 168 CG2 THR A 23 -26.392 3.523 17.774 1.00 90.80 C ANISOU 168 CG2 THR A 23 18302 8067 8129 3912 438 1109 C ATOM 169 OG1 THR A 23 -28.139 3.702 19.382 1.00 79.29 O ANISOU 169 OG1 THR A 23 17258 6197 6671 3347 701 1252 O ATOM 170 N VAL A 24 -28.942 3.918 14.983 1.00 83.82 N ANISOU 170 N VAL A 24 17151 6945 7753 2790 677 659 N ATOM 171 CA VAL A 24 -28.769 3.870 13.527 1.00 82.51 C ANISOU 171 CA VAL A 24 16808 6865 7676 2792 637 484 C ATOM 172 C VAL A 24 -29.362 5.095 12.797 1.00 82.35 C ANISOU 172 C VAL A 24 16295 7173 7821 2433 568 363 C ATOM 173 O VAL A 24 -28.868 5.426 11.721 1.00 82.69 O ANISOU 173 O VAL A 24 16041 7460 7918 2494 474 248 O ATOM 174 CB VAL A 24 -29.358 2.578 12.896 1.00 82.57 C ANISOU 174 CB VAL A 24 17271 6409 7693 2694 808 402 C ATOM 175 CG1 VAL A 24 -28.620 1.324 13.393 1.00 85.54 C ANISOU 175 CG1 VAL A 24 18180 6422 7901 3060 891 545 C ATOM 176 CG2 VAL A 24 -30.884 2.418 13.040 1.00 82.76 C ANISOU 176 CG2 VAL A 24 17368 6240 7837 2148 952 340 C ATOM 177 N LEU A 25 -30.354 5.775 13.404 1.00 81.85 N ANISOU 177 N LEU A 25 16139 7127 7833 2068 619 390 N ATOM 178 CA LEU A 25 -30.918 7.038 12.915 1.00 81.60 C ANISOU 178 CA LEU A 25 15643 7412 7949 1765 549 295 C ATOM 179 C LEU A 25 -29.998 8.254 13.147 1.00 80.84 C ANISOU 179 C LEU A 25 15134 7739 7841 1953 376 337 C ATOM 180 O LEU A 25 -30.230 9.279 12.509 1.00 78.89 O ANISOU 180 O LEU A 25 14499 7768 7709 1767 305 258 O ATOM 181 CB LEU A 25 -32.307 7.276 13.551 1.00 82.24 C ANISOU 181 CB LEU A 25 15743 7395 8111 1344 662 308 C ATOM 182 CG LEU A 25 -33.430 6.385 12.977 1.00 86.96 C ANISOU 182 CG LEU A 25 16645 7636 8761 1035 834 220 C ATOM 183 CD1 LEU A 25 -34.697 6.455 13.856 1.00 86.42 C ANISOU 183 CD1 LEU A 25 16523 7539 8773 623 941 232 C ATOM 184 CD2 LEU A 25 -33.726 6.700 11.494 1.00 87.12 C ANISOU 184 CD2 LEU A 25 16519 7715 8866 935 798 35 C ATOM 185 N ARG A 26 -28.974 8.126 14.012 1.00 83.64 N ANISOU 185 N ARG A 26 15567 8154 8057 2308 307 457 N ATOM 186 CA ARG A 26 -27.912 9.123 14.173 1.00 81.19 C ANISOU 186 CA ARG A 26 14862 8256 7729 2503 137 467 C ATOM 187 C ARG A 26 -26.720 8.865 13.239 1.00 82.92 C ANISOU 187 C ARG A 26 14957 8624 7925 2796 54 391 C ATOM 188 O ARG A 26 -26.053 9.830 12.875 1.00 82.90 O ANISOU 188 O ARG A 26 14552 8978 7968 2828 -62 339 O ATOM 189 CB ARG A 26 -27.428 9.177 15.632 1.00 79.56 C ANISOU 189 CB ARG A 26 14747 8107 7373 2741 81 614 C ATOM 190 CG ARG A 26 -28.502 9.651 16.620 1.00 79.20 C ANISOU 190 CG ARG A 26 14779 7977 7335 2467 158 690 C ATOM 191 CD ARG A 26 -27.943 9.955 18.016 1.00 81.39 C ANISOU 191 CD ARG A 26 15099 8380 7447 2714 77 821 C ATOM 192 NE ARG A 26 -27.460 8.756 18.713 1.00 85.13 N ANISOU 192 NE ARG A 26 16016 8589 7740 3039 123 942 N ATOM 193 CZ ARG A 26 -28.228 7.939 19.449 1.00 86.37 C ANISOU 193 CZ ARG A 26 16579 8427 7810 2968 264 1058 C ATOM 194 NH1 ARG A 26 -29.543 8.153 19.556 1.00 85.02 N1+ ANISOU 194 NH1 ARG A 26 16399 8184 7721 2576 376 1058 N1+ ATOM 195 NH2 ARG A 26 -27.679 6.901 20.092 1.00 89.17 N1+ ANISOU 195 NH2 ARG A 26 17355 8535 7991 3297 304 1179 N1+ ATOM 196 N ILE A 27 -26.481 7.600 12.852 1.00 83.48 N ANISOU 196 N ILE A 27 15377 8420 7923 3008 124 380 N ATOM 197 CA ILE A 27 -25.438 7.213 11.896 1.00 83.20 C ANISOU 197 CA ILE A 27 15246 8507 7858 3296 68 296 C ATOM 198 C ILE A 27 -25.871 7.441 10.432 1.00 79.94 C ANISOU 198 C ILE A 27 14656 8141 7578 3025 99 136 C ATOM 199 O ILE A 27 -25.024 7.788 9.611 1.00 64.52 O ANISOU 199 O ILE A 27 12440 6442 5634 3165 28 55 O ATOM 200 CB ILE A 27 -25.010 5.726 12.100 1.00 89.97 C ANISOU 200 CB ILE A 27 16570 9034 8581 3650 140 341 C ATOM 201 CG1 ILE A 27 -24.365 5.505 13.490 1.00 92.56 C ANISOU 201 CG1 ILE A 27 17088 9324 8757 3927 104 518 C ATOM 202 CG2 ILE A 27 -24.107 5.132 10.992 1.00 91.18 C ANISOU 202 CG2 ILE A 27 16618 9334 8692 3993 86 252 C ATOM 203 CD1 ILE A 27 -23.111 6.348 13.777 1.00 92.36 C ANISOU 203 CD1 ILE A 27 16664 9760 8669 4184 -79 555 C ATOM 204 N LEU A 28 -27.177 7.282 10.148 1.00 78.31 N ANISOU 204 N LEU A 28 14576 7714 7465 2637 203 87 N ATOM 205 CA LEU A 28 -27.819 7.503 8.849 1.00 75.53 C ANISOU 205 CA LEU A 28 14079 7402 7217 2382 225 -68 C ATOM 206 C LEU A 28 -27.497 8.866 8.189 1.00 69.77 C ANISOU 206 C LEU A 28 12847 7100 6563 2310 108 -110 C ATOM 207 O LEU A 28 -27.003 8.838 7.062 1.00 69.29 O ANISOU 207 O LEU A 28 12648 7174 6505 2383 81 -213 O ATOM 208 CB LEU A 28 -29.337 7.218 8.990 1.00 75.17 C ANISOU 208 CB LEU A 28 14204 7100 7256 1958 342 -108 C ATOM 209 CG LEU A 28 -30.226 7.534 7.761 1.00 76.47 C ANISOU 209 CG LEU A 28 14197 7335 7524 1651 351 -270 C ATOM 210 CD1 LEU A 28 -29.777 6.773 6.494 1.00 78.34 C ANISOU 210 CD1 LEU A 28 14588 7473 7706 1824 373 -396 C ATOM 211 CD2 LEU A 28 -31.715 7.297 8.092 1.00 78.33 C ANISOU 211 CD2 LEU A 28 14574 7351 7837 1236 460 -307 C ATOM 212 N PRO A 29 -27.719 10.020 8.867 1.00 66.62 N ANISOU 212 N PRO A 29 12178 6917 6219 2169 45 -39 N ATOM 213 CA PRO A 29 -27.367 11.331 8.296 1.00 64.95 C ANISOU 213 CA PRO A 29 11520 7083 6076 2113 -54 -77 C ATOM 214 C PRO A 29 -25.870 11.563 8.051 1.00 64.74 C ANISOU 214 C PRO A 29 11321 7307 5972 2465 -140 -73 C ATOM 215 O PRO A 29 -25.554 12.246 7.081 1.00 67.31 O ANISOU 215 O PRO A 29 11349 7891 6335 2448 -186 -137 O ATOM 216 CB PRO A 29 -27.954 12.352 9.279 1.00 62.32 C ANISOU 216 CB PRO A 29 11014 6862 5803 1917 -85 5 C ATOM 217 CG PRO A 29 -28.073 11.606 10.593 1.00 65.48 C ANISOU 217 CG PRO A 29 11719 7046 6114 2034 -44 109 C ATOM 218 CD PRO A 29 -28.419 10.195 10.139 1.00 67.45 C ANISOU 218 CD PRO A 29 12374 6933 6322 2055 70 74 C ATOM 219 N LEU A 30 -24.989 10.972 8.880 1.00 63.34 N ANISOU 219 N LEU A 30 11317 7073 5677 2790 -161 2 N ATOM 220 CA LEU A 30 -23.532 11.034 8.719 1.00 62.83 C ANISOU 220 CA LEU A 30 11078 7265 5530 3150 -243 -6 C ATOM 221 C LEU A 30 -23.067 10.317 7.440 1.00 64.99 C ANISOU 221 C LEU A 30 11414 7499 5781 3288 -196 -118 C ATOM 222 O LEU A 30 -22.264 10.877 6.696 1.00 64.85 O ANISOU 222 O LEU A 30 11103 7780 5756 3412 -246 -173 O ATOM 223 CB LEU A 30 -22.812 10.431 9.948 1.00 65.81 C ANISOU 223 CB LEU A 30 11654 7580 5770 3493 -280 101 C ATOM 224 CG LEU A 30 -23.231 10.996 11.322 1.00 66.95 C ANISOU 224 CG LEU A 30 11798 7737 5904 3380 -318 212 C ATOM 225 CD1 LEU A 30 -22.599 10.173 12.466 1.00 70.91 C ANISOU 225 CD1 LEU A 30 12535 8169 6238 3753 -356 322 C ATOM 226 CD2 LEU A 30 -22.975 12.511 11.463 1.00 66.53 C ANISOU 226 CD2 LEU A 30 11289 8066 5922 3228 -419 196 C ATOM 227 N VAL A 31 -23.629 9.122 7.182 1.00 67.75 N ANISOU 227 N VAL A 31 12148 7482 6114 3255 -91 -160 N ATOM 228 CA VAL A 31 -23.427 8.341 5.958 1.00 69.77 C ANISOU 228 CA VAL A 31 12493 7676 6341 3367 -37 -287 C ATOM 229 C VAL A 31 -23.935 9.074 4.697 1.00 66.24 C ANISOU 229 C VAL A 31 11773 7405 5989 3057 -40 -391 C ATOM 230 O VAL A 31 -23.284 8.983 3.655 1.00 65.51 O ANISOU 230 O VAL A 31 11511 7509 5870 3174 -49 -477 O ATOM 231 CB VAL A 31 -24.098 6.937 6.080 1.00 73.64 C ANISOU 231 CB VAL A 31 13498 7695 6786 3390 84 -316 C ATOM 232 CG1 VAL A 31 -24.255 6.148 4.761 1.00 67.80 C ANISOU 232 CG1 VAL A 31 12864 6882 6014 3484 144 -470 C ATOM 233 CG2 VAL A 31 -23.347 6.065 7.103 1.00 68.74 C ANISOU 233 CG2 VAL A 31 13169 6898 6049 3746 88 -193 C ATOM 234 N VAL A 32 -25.039 9.834 4.831 1.00 64.96 N ANISOU 234 N VAL A 32 11563 7190 5928 2672 -29 -381 N ATOM 235 CA VAL A 32 -25.563 10.699 3.775 1.00 60.60 C ANISOU 235 CA VAL A 32 10750 6817 5457 2391 -43 -462 C ATOM 236 C VAL A 32 -24.645 11.911 3.485 1.00 57.12 C ANISOU 236 C VAL A 32 9888 6784 5030 2467 -128 -433 C ATOM 237 O VAL A 32 -24.521 12.265 2.314 1.00 58.78 O ANISOU 237 O VAL A 32 9914 7181 5239 2439 -131 -509 O ATOM 238 CB VAL A 32 -27.029 11.152 4.037 1.00 60.06 C ANISOU 238 CB VAL A 32 10690 6638 5492 1999 -22 -443 C ATOM 239 CG1 VAL A 32 -27.558 12.238 3.075 1.00 56.12 C ANISOU 239 CG1 VAL A 32 9893 6363 5067 1745 -57 -504 C ATOM 240 CG2 VAL A 32 -27.991 9.951 3.983 1.00 61.75 C ANISOU 240 CG2 VAL A 32 11309 6458 5695 1878 81 -498 C ATOM 241 N LEU A 33 -23.965 12.481 4.494 1.00 55.64 N ANISOU 241 N LEU A 33 9550 6744 4847 2557 -192 -327 N ATOM 242 CA LEU A 33 -22.946 13.515 4.257 1.00 57.65 C ANISOU 242 CA LEU A 33 9418 7378 5110 2630 -264 -310 C ATOM 243 C LEU A 33 -21.715 12.964 3.516 1.00 64.47 C ANISOU 243 C LEU A 33 10231 8391 5875 2975 -265 -364 C ATOM 244 O LEU A 33 -21.117 13.697 2.732 1.00 66.32 O ANISOU 244 O LEU A 33 10154 8932 6113 2993 -286 -393 O ATOM 245 CB LEU A 33 -22.485 14.220 5.554 1.00 58.24 C ANISOU 245 CB LEU A 33 9357 7570 5200 2639 -335 -207 C ATOM 246 CG LEU A 33 -23.569 14.943 6.382 1.00 52.24 C ANISOU 246 CG LEU A 33 8556 6747 4544 2304 -337 -156 C ATOM 247 CD1 LEU A 33 -22.925 15.810 7.482 1.00 50.90 C ANISOU 247 CD1 LEU A 33 8151 6798 4390 2307 -416 -86 C ATOM 248 CD2 LEU A 33 -24.565 15.747 5.527 1.00 50.50 C ANISOU 248 CD2 LEU A 33 8195 6578 4415 2024 -310 -211 C ATOM 249 N GLY A 34 -21.379 11.685 3.736 1.00 66.44 N ANISOU 249 N GLY A 34 10787 8426 6031 3254 -231 -375 N ATOM 250 CA GLY A 34 -20.238 11.014 3.117 1.00 69.41 C ANISOU 250 CA GLY A 34 11128 8937 6308 3613 -222 -434 C ATOM 251 C GLY A 34 -20.437 10.863 1.603 1.00 70.74 C ANISOU 251 C GLY A 34 11266 9140 6470 3548 -156 -559 C ATOM 252 O GLY A 34 -19.513 11.162 0.845 1.00 71.94 O ANISOU 252 O GLY A 34 11140 9600 6592 3660 -162 -603 O ATOM 253 N VAL A 35 -21.641 10.446 1.163 1.00 69.66 N ANISOU 253 N VAL A 35 11415 8701 6353 3356 -89 -625 N ATOM 254 CA VAL A 35 -21.979 10.333 -0.260 1.00 72.14 C ANISOU 254 CA VAL A 35 11720 9048 6644 3278 -34 -755 C ATOM 255 C VAL A 35 -22.251 11.703 -0.918 1.00 72.10 C ANISOU 255 C VAL A 35 11349 9338 6706 3002 -71 -746 C ATOM 256 O VAL A 35 -21.905 11.867 -2.085 1.00 74.71 O ANISOU 256 O VAL A 35 11524 9871 6991 3031 -45 -820 O ATOM 257 CB VAL A 35 -23.173 9.380 -0.547 1.00 75.49 C ANISOU 257 CB VAL A 35 12537 9079 7066 3116 39 -844 C ATOM 258 CG1 VAL A 35 -22.880 7.951 -0.059 1.00 77.87 C ANISOU 258 CG1 VAL A 35 13238 9055 7293 3408 93 -843 C ATOM 259 CG2 VAL A 35 -24.543 9.860 -0.038 1.00 76.16 C ANISOU 259 CG2 VAL A 35 12631 9047 7261 2721 20 -794 C ATOM 260 N THR A 36 -22.800 12.672 -0.160 1.00 69.82 N ANISOU 260 N THR A 36 10929 9081 6519 2746 -122 -652 N ATOM 261 CA THR A 36 -23.019 14.048 -0.624 1.00 67.96 C ANISOU 261 CA THR A 36 10364 9111 6348 2511 -153 -626 C ATOM 262 C THR A 36 -21.702 14.836 -0.781 1.00 68.95 C ANISOU 262 C THR A 36 10162 9590 6447 2679 -176 -595 C ATOM 263 O THR A 36 -21.629 15.690 -1.662 1.00 65.79 O ANISOU 263 O THR A 36 9519 9422 6057 2559 -166 -601 O ATOM 264 CB THR A 36 -23.961 14.845 0.319 1.00 66.54 C ANISOU 264 CB THR A 36 10135 8867 6280 2232 -195 -536 C ATOM 265 CG2 THR A 36 -24.268 16.291 -0.104 1.00 63.00 C ANISOU 265 CG2 THR A 36 9391 8650 5897 1997 -218 -507 C ATOM 266 OG1 THR A 36 -25.206 14.185 0.408 1.00 68.14 O ANISOU 266 OG1 THR A 36 10625 8758 6506 2065 -162 -573 O ATOM 267 N PHE A 37 -20.682 14.509 0.033 1.00 72.48 N ANISOU 267 N PHE A 37 10597 10092 6850 2957 -203 -562 N ATOM 268 CA PHE A 37 -19.317 15.018 -0.093 1.00 71.39 C ANISOU 268 CA PHE A 37 10130 10314 6680 3124 -221 -554 C ATOM 269 C PHE A 37 -18.647 14.596 -1.408 1.00 75.25 C ANISOU 269 C PHE A 37 10586 10932 7072 3317 -150 -656 C ATOM 270 O PHE A 37 -18.305 15.468 -2.203 1.00 76.97 O ANISOU 270 O PHE A 37 10532 11425 7287 3238 -121 -672 O ATOM 271 CB PHE A 37 -18.485 14.676 1.169 1.00 66.96 C ANISOU 271 CB PHE A 37 9555 9802 6084 3386 -285 -500 C ATOM 272 CG PHE A 37 -16.974 14.819 1.043 1.00 65.93 C ANISOU 272 CG PHE A 37 9093 10056 5904 3600 -304 -519 C ATOM 273 CD1 PHE A 37 -16.383 16.098 0.988 1.00 61.54 C ANISOU 273 CD1 PHE A 37 8172 9798 5411 3403 -328 -491 C ATOM 274 CD2 PHE A 37 -16.164 13.684 0.820 1.00 65.67 C ANISOU 274 CD2 PHE A 37 9109 10084 5760 3996 -289 -571 C ATOM 275 CE1 PHE A 37 -15.018 16.229 0.773 1.00 65.34 C ANISOU 275 CE1 PHE A 37 8328 10648 5849 3565 -335 -520 C ATOM 276 CE2 PHE A 37 -14.801 13.834 0.604 1.00 63.62 C ANISOU 276 CE2 PHE A 37 8507 10213 5454 4189 -304 -598 C ATOM 277 CZ PHE A 37 -14.230 15.101 0.585 1.00 62.37 C ANISOU 277 CZ PHE A 37 7969 10365 5363 3958 -326 -576 C ATOM 278 N VAL A 38 -18.478 13.276 -1.603 1.00 75.66 N ANISOU 278 N VAL A 38 10930 10779 7040 3573 -109 -726 N ATOM 279 CA VAL A 38 -17.728 12.709 -2.726 1.00 76.25 C ANISOU 279 CA VAL A 38 10988 10975 7010 3801 -34 -835 C ATOM 280 C VAL A 38 -18.411 12.916 -4.096 1.00 75.34 C ANISOU 280 C VAL A 38 10875 10863 6887 3551 23 -907 C ATOM 281 O VAL A 38 -17.712 13.246 -5.051 1.00 78.63 O ANISOU 281 O VAL A 38 11069 11556 7251 3579 72 -950 O ATOM 282 CB VAL A 38 -17.393 11.207 -2.494 1.00 77.53 C ANISOU 282 CB VAL A 38 11504 10873 7081 4146 2 -896 C ATOM 283 CG1 VAL A 38 -18.615 10.273 -2.518 1.00 77.75 C ANISOU 283 CG1 VAL A 38 11939 10457 7146 3982 10 -895 C ATOM 284 CG2 VAL A 38 -16.319 10.679 -3.461 1.00 78.02 C ANISOU 284 CG2 VAL A 38 11595 11014 7033 4355 95 -1031 C ATOM 285 N LEU A 39 -19.750 12.799 -4.157 1.00 71.51 N ANISOU 285 N LEU A 39 10631 10092 6446 3300 18 -921 N ATOM 286 CA LEU A 39 -20.542 13.093 -5.358 1.00 69.72 C ANISOU 286 CA LEU A 39 10400 9891 6200 3064 51 -991 C ATOM 287 C LEU A 39 -20.739 14.604 -5.580 1.00 71.73 C ANISOU 287 C LEU A 39 10312 10428 6515 2824 23 -902 C ATOM 288 O LEU A 39 -21.059 14.999 -6.699 1.00 74.23 O ANISOU 288 O LEU A 39 10507 10924 6772 2748 63 -940 O ATOM 289 CB LEU A 39 -21.920 12.397 -5.275 1.00 67.09 C ANISOU 289 CB LEU A 39 10379 9211 5901 2842 43 -1037 C ATOM 290 CG LEU A 39 -21.875 10.854 -5.199 1.00 70.81 C ANISOU 290 CG LEU A 39 11254 9336 6315 3017 92 -1135 C ATOM 291 CD1 LEU A 39 -23.279 10.278 -4.915 1.00 72.21 C ANISOU 291 CD1 LEU A 39 11686 9223 6527 2716 96 -1203 C ATOM 292 CD2 LEU A 39 -21.221 10.221 -6.445 1.00 73.38 C ANISOU 292 CD2 LEU A 39 11648 9728 6506 3306 168 -1263 C ATOM 293 N GLY A 40 -20.559 15.416 -4.526 1.00 73.20 N ANISOU 293 N GLY A 40 10354 10649 6809 2709 -41 -782 N ATOM 294 CA GLY A 40 -20.702 16.865 -4.573 1.00 74.04 C ANISOU 294 CA GLY A 40 10177 10971 6983 2469 -60 -695 C ATOM 295 C GLY A 40 -19.450 17.493 -5.183 1.00 75.43 C ANISOU 295 C GLY A 40 10052 11497 7112 2574 -14 -685 C ATOM 296 O GLY A 40 -19.559 18.212 -6.173 1.00 74.94 O ANISOU 296 O GLY A 40 9835 11605 7035 2419 24 -664 O ATOM 297 N VAL A 41 -18.269 17.213 -4.605 1.00 78.75 N ANISOU 297 N VAL A 41 10381 12040 7503 2839 -13 -697 N ATOM 298 CA VAL A 41 -16.995 17.794 -5.036 1.00 80.56 C ANISOU 298 CA VAL A 41 10285 12631 7692 2923 38 -695 C ATOM 299 C VAL A 41 -16.502 17.259 -6.398 1.00 82.32 C ANISOU 299 C VAL A 41 10525 12964 7787 3041 138 -792 C ATOM 300 O VAL A 41 -15.852 18.014 -7.119 1.00 81.95 O ANISOU 300 O VAL A 41 10232 13200 7705 2982 208 -782 O ATOM 301 CB VAL A 41 -15.868 17.616 -3.978 1.00 82.02 C ANISOU 301 CB VAL A 41 10335 12955 7873 3182 -2 -692 C ATOM 302 CG1 VAL A 41 -16.237 18.279 -2.637 1.00 80.71 C ANISOU 302 CG1 VAL A 41 10148 12701 7816 3048 -102 -600 C ATOM 303 CG2 VAL A 41 -15.368 16.169 -3.784 1.00 84.65 C ANISOU 303 CG2 VAL A 41 10909 13143 8110 3542 8 -776 C ATOM 304 N LEU A 42 -16.844 16.005 -6.749 1.00 81.34 N ANISOU 304 N LEU A 42 10704 12616 7587 3196 158 -892 N ATOM 305 CA LEU A 42 -16.523 15.422 -8.054 1.00 82.30 C ANISOU 305 CA LEU A 42 10870 12830 7571 3316 256 -1003 C ATOM 306 C LEU A 42 -17.582 15.764 -9.111 1.00 77.65 C ANISOU 306 C LEU A 42 10335 12212 6957 3031 273 -1005 C ATOM 307 O LEU A 42 -17.200 16.057 -10.240 1.00 78.58 O ANISOU 307 O LEU A 42 10297 12571 6990 2995 350 -1016 O ATOM 308 CB LEU A 42 -16.349 13.891 -7.951 1.00 86.66 C ANISOU 308 CB LEU A 42 11745 13139 8044 3603 277 -1124 C ATOM 309 CG LEU A 42 -15.147 13.432 -7.094 1.00 91.26 C ANISOU 309 CG LEU A 42 12312 13752 8613 3968 266 -1130 C ATOM 310 CD1 LEU A 42 -15.154 11.902 -6.906 1.00 94.34 C ANISOU 310 CD1 LEU A 42 13075 13856 8914 4248 306 -1250 C ATOM 311 CD2 LEU A 42 -13.795 13.933 -7.646 1.00 92.99 C ANISOU 311 CD2 LEU A 42 12151 14398 8784 4139 320 -1131 C ATOM 312 N GLY A 43 -18.876 15.730 -8.748 1.00 74.14 N ANISOU 312 N GLY A 43 10105 11489 6576 2830 203 -994 N ATOM 313 CA GLY A 43 -19.983 15.949 -9.683 1.00 73.30 C ANISOU 313 CA GLY A 43 10050 11366 6435 2579 198 -1004 C ATOM 314 C GLY A 43 -20.044 17.411 -10.137 1.00 73.88 C ANISOU 314 C GLY A 43 9841 11690 6539 2379 207 -878 C ATOM 315 O GLY A 43 -20.107 17.667 -11.338 1.00 78.40 O ANISOU 315 O GLY A 43 10350 12433 7004 2326 265 -890 O ATOM 316 N ASN A 44 -19.985 18.359 -9.187 1.00 71.05 N ANISOU 316 N ASN A 44 9330 11347 6320 2265 157 -754 N ATOM 317 CA ASN A 44 -19.947 19.800 -9.463 1.00 69.63 C ANISOU 317 CA ASN A 44 8906 11369 6180 2071 177 -631 C ATOM 318 C ASN A 44 -18.551 20.275 -9.898 1.00 69.54 C ANISOU 318 C ASN A 44 8656 11671 6095 2186 282 -628 C ATOM 319 O ASN A 44 -18.473 21.306 -10.561 1.00 70.36 O ANISOU 319 O ASN A 44 8623 11953 6157 2050 346 -561 O ATOM 320 CB ASN A 44 -20.437 20.599 -8.239 1.00 67.94 C ANISOU 320 CB ASN A 44 8606 11078 6130 1925 105 -520 C ATOM 321 CG ASN A 44 -21.906 20.330 -7.912 1.00 65.91 C ANISOU 321 CG ASN A 44 8550 10544 5948 1779 18 -511 C ATOM 322 ND2 ASN A 44 -22.168 19.556 -6.859 1.00 63.70 N ANISOU 322 ND2 ASN A 44 8404 10070 5730 1859 -33 -537 N ATOM 323 OD1 ASN A 44 -22.794 20.825 -8.601 1.00 66.18 O ANISOU 323 OD1 ASN A 44 8617 10552 5978 1599 0 -479 O ATOM 324 N GLY A 45 -17.490 19.512 -9.578 1.00 68.40 N ANISOU 324 N GLY A 45 8457 11604 5928 2440 307 -696 N ATOM 325 CA GLY A 45 -16.133 19.751 -10.077 1.00 67.02 C ANISOU 325 CA GLY A 45 8036 11753 5674 2563 417 -716 C ATOM 326 C GLY A 45 -16.039 19.456 -11.585 1.00 68.80 C ANISOU 326 C GLY A 45 8324 12086 5732 2616 520 -789 C ATOM 327 O GLY A 45 -15.324 20.161 -12.295 1.00 68.95 O ANISOU 327 O GLY A 45 8141 12373 5685 2562 627 -753 O ATOM 328 N LEU A 46 -16.799 18.457 -12.074 1.00 69.88 N ANISOU 328 N LEU A 46 8751 12012 5790 2708 495 -897 N ATOM 329 CA LEU A 46 -16.946 18.136 -13.494 1.00 72.16 C ANISOU 329 CA LEU A 46 9129 12388 5902 2742 581 -981 C ATOM 330 C LEU A 46 -17.816 19.159 -14.245 1.00 70.04 C ANISOU 330 C LEU A 46 8811 12193 5606 2460 585 -876 C ATOM 331 O LEU A 46 -17.543 19.381 -15.422 1.00 71.50 O ANISOU 331 O LEU A 46 8900 12610 5658 2450 693 -867 O ATOM 332 CB LEU A 46 -17.501 16.703 -13.661 1.00 74.46 C ANISOU 332 CB LEU A 46 9761 12404 6125 2858 541 -1132 C ATOM 333 CG LEU A 46 -16.474 15.588 -13.352 1.00 76.86 C ANISOU 333 CG LEU A 46 10178 12631 6394 3200 574 -1258 C ATOM 334 CD1 LEU A 46 -17.172 14.220 -13.186 1.00 78.72 C ANISOU 334 CD1 LEU A 46 10796 12526 6590 3242 532 -1393 C ATOM 335 CD2 LEU A 46 -15.329 15.543 -14.384 1.00 76.88 C ANISOU 335 CD2 LEU A 46 10027 12934 6251 3428 715 -1333 C ATOM 336 N VAL A 47 -18.802 19.793 -13.579 1.00 67.61 N ANISOU 336 N VAL A 47 8574 11698 5415 2243 475 -789 N ATOM 337 CA VAL A 47 -19.569 20.907 -14.156 1.00 67.62 C ANISOU 337 CA VAL A 47 8536 11760 5395 2003 468 -674 C ATOM 338 C VAL A 47 -18.711 22.183 -14.266 1.00 67.39 C ANISOU 338 C VAL A 47 8235 11970 5400 1910 559 -534 C ATOM 339 O VAL A 47 -18.761 22.839 -15.303 1.00 67.77 O ANISOU 339 O VAL A 47 8229 12176 5342 1813 636 -461 O ATOM 340 CB VAL A 47 -20.853 21.261 -13.351 1.00 68.07 C ANISOU 340 CB VAL A 47 8709 11570 5582 1818 331 -619 C ATOM 341 CG1 VAL A 47 -21.583 22.529 -13.857 1.00 66.75 C ANISOU 341 CG1 VAL A 47 8489 11475 5398 1604 319 -485 C ATOM 342 CG2 VAL A 47 -21.843 20.086 -13.310 1.00 69.14 C ANISOU 342 CG2 VAL A 47 9115 11481 5674 1868 260 -769 C ATOM 343 N ILE A 48 -17.923 22.492 -13.221 1.00 68.88 N ANISOU 343 N ILE A 48 8256 12188 5727 1931 557 -495 N ATOM 344 CA ILE A 48 -16.980 23.615 -13.193 1.00 70.72 C ANISOU 344 CA ILE A 48 8221 12655 5996 1829 655 -390 C ATOM 345 C ILE A 48 -15.902 23.519 -14.293 1.00 72.88 C ANISOU 345 C ILE A 48 8378 13212 6103 1948 813 -441 C ATOM 346 O ILE A 48 -15.532 24.549 -14.853 1.00 73.70 O ANISOU 346 O ILE A 48 8346 13500 6156 1808 928 -344 O ATOM 347 CB ILE A 48 -16.332 23.781 -11.781 1.00 70.75 C ANISOU 347 CB ILE A 48 8061 12661 6158 1852 611 -381 C ATOM 348 CG1 ILE A 48 -17.371 24.344 -10.782 1.00 71.02 C ANISOU 348 CG1 ILE A 48 8182 12449 6352 1679 484 -299 C ATOM 349 CG2 ILE A 48 -15.042 24.634 -11.722 1.00 70.65 C ANISOU 349 CG2 ILE A 48 7746 12936 6162 1772 731 -324 C ATOM 350 CD1 ILE A 48 -17.036 24.068 -9.310 1.00 71.63 C ANISOU 350 CD1 ILE A 48 8143 12509 6565 1715 420 -305 C ATOM 351 N TRP A 49 -15.472 22.287 -14.616 1.00 75.07 N ANISOU 351 N TRP A 49 8721 13517 6285 2212 834 -594 N ATOM 352 CA TRP A 49 -14.572 21.990 -15.725 1.00 80.63 C ANISOU 352 CA TRP A 49 9310 14502 6824 2357 993 -662 C ATOM 353 C TRP A 49 -15.277 22.083 -17.090 1.00 83.01 C ANISOU 353 C TRP A 49 9771 14833 6939 2303 1051 -666 C ATOM 354 O TRP A 49 -14.825 22.851 -17.938 1.00 85.75 O ANISOU 354 O TRP A 49 9988 15421 7171 2237 1196 -607 O ATOM 355 CB TRP A 49 -13.920 20.612 -15.499 1.00 84.53 C ANISOU 355 CB TRP A 49 9835 15004 7278 2691 995 -828 C ATOM 356 CG TRP A 49 -12.912 20.151 -16.514 1.00 90.82 C ANISOU 356 CG TRP A 49 10496 16102 7911 2878 1165 -915 C ATOM 357 CD1 TRP A 49 -11.934 20.907 -17.067 1.00 94.76 C ANISOU 357 CD1 TRP A 49 10680 16937 8386 2828 1309 -864 C ATOM 358 CD2 TRP A 49 -12.702 18.800 -17.026 1.00 95.43 C ANISOU 358 CD2 TRP A 49 11253 16680 8326 3144 1220 -1080 C ATOM 359 CE2 TRP A 49 -11.566 18.810 -17.891 1.00 99.94 C ANISOU 359 CE2 TRP A 49 11592 17608 8775 3260 1401 -1117 C ATOM 360 CE3 TRP A 49 -13.352 17.560 -16.835 1.00 96.07 C ANISOU 360 CE3 TRP A 49 11669 16484 8348 3283 1144 -1208 C ATOM 361 NE1 TRP A 49 -11.148 20.125 -17.887 1.00 99.37 N ANISOU 361 NE1 TRP A 49 11216 17745 8796 3052 1454 -981 N ATOM 362 CZ2 TRP A 49 -11.091 17.645 -18.519 1.00102.79 C ANISOU 362 CZ2 TRP A 49 12045 18058 8952 3533 1505 -1277 C ATOM 363 CZ3 TRP A 49 -12.883 16.383 -17.452 1.00 98.37 C ANISOU 363 CZ3 TRP A 49 12070 16846 8461 3541 1244 -1372 C ATOM 364 CH2 TRP A 49 -11.748 16.423 -18.284 1.00101.69 C ANISOU 364 CH2 TRP A 49 12254 17626 8757 3676 1422 -1405 C ATOM 365 N VAL A 50 -16.351 21.296 -17.288 1.00 82.10 N ANISOU 365 N VAL A 50 9934 14481 6778 2319 944 -737 N ATOM 366 CA VAL A 50 -17.040 21.164 -18.574 1.00 80.68 C ANISOU 366 CA VAL A 50 9913 14345 6396 2288 978 -770 C ATOM 367 C VAL A 50 -17.800 22.440 -18.979 1.00 79.25 C ANISOU 367 C VAL A 50 9713 14183 6217 2024 959 -588 C ATOM 368 O VAL A 50 -17.434 23.038 -19.985 1.00 82.46 O ANISOU 368 O VAL A 50 10042 14804 6484 1964 1083 -506 O ATOM 369 CB VAL A 50 -17.966 19.914 -18.652 1.00 77.73 C ANISOU 369 CB VAL A 50 9838 13725 5972 2381 868 -932 C ATOM 370 CG1 VAL A 50 -18.884 19.851 -19.894 1.00 78.17 C ANISOU 370 CG1 VAL A 50 10050 13843 5809 2326 880 -976 C ATOM 371 CG2 VAL A 50 -17.127 18.624 -18.600 1.00 78.09 C ANISOU 371 CG2 VAL A 50 9939 13739 5994 2673 910 -1106 C ATOM 372 N ALA A 51 -18.806 22.856 -18.192 1.00 74.97 N ANISOU 372 N ALA A 51 9249 13414 5822 1874 812 -516 N ATOM 373 CA ALA A 51 -19.597 24.065 -18.449 1.00 75.70 C ANISOU 373 CA ALA A 51 9346 13502 5914 1658 781 -345 C ATOM 374 C ALA A 51 -18.794 25.375 -18.328 1.00 78.54 C ANISOU 374 C ALA A 51 9487 14014 6339 1532 901 -173 C ATOM 375 O ALA A 51 -19.150 26.347 -18.992 1.00 79.51 O ANISOU 375 O ALA A 51 9612 14219 6380 1402 957 -29 O ATOM 376 CB ALA A 51 -20.825 24.095 -17.522 1.00 70.92 C ANISOU 376 CB ALA A 51 8848 12630 5467 1544 605 -318 C ATOM 377 N GLY A 52 -17.734 25.381 -17.502 1.00 78.46 N ANISOU 377 N GLY A 52 9295 14048 6469 1566 945 -188 N ATOM 378 CA GLY A 52 -16.955 26.582 -17.213 1.00 76.76 C ANISOU 378 CA GLY A 52 8865 13966 6335 1412 1056 -48 C ATOM 379 C GLY A 52 -15.772 26.800 -18.169 1.00 76.41 C ANISOU 379 C GLY A 52 8674 14224 6136 1441 1261 -41 C ATOM 380 O GLY A 52 -15.309 27.938 -18.247 1.00 77.63 O ANISOU 380 O GLY A 52 8743 14479 6274 1261 1379 110 O ATOM 381 N PHE A 53 -15.266 25.761 -18.867 1.00 78.54 N ANISOU 381 N PHE A 53 8923 14633 6288 1666 1318 -201 N ATOM 382 CA PHE A 53 -14.056 25.865 -19.701 1.00 85.87 C ANISOU 382 CA PHE A 53 9670 15878 7079 1714 1528 -215 C ATOM 383 C PHE A 53 -14.160 25.115 -21.038 1.00 89.33 C ANISOU 383 C PHE A 53 10246 16435 7260 1882 1605 -317 C ATOM 384 O PHE A 53 -13.778 25.690 -22.058 1.00 92.05 O ANISOU 384 O PHE A 53 10475 17045 7457 1874 1797 -289 O ATOM 385 CB PHE A 53 -12.791 25.415 -18.931 1.00 70.84 C ANISOU 385 CB PHE A 53 7511 14126 5279 1848 1570 -318 C ATOM 386 CG PHE A 53 -12.447 26.230 -17.696 1.00 69.38 C ANISOU 386 CG PHE A 53 7159 13878 5323 1679 1509 -236 C ATOM 387 CD1 PHE A 53 -11.822 27.489 -17.821 1.00 70.28 C ANISOU 387 CD1 PHE A 53 7057 14159 5486 1447 1645 -117 C ATOM 388 CD2 PHE A 53 -12.897 25.812 -16.427 1.00 74.00 C ANISOU 388 CD2 PHE A 53 7817 14233 6068 1738 1323 -282 C ATOM 389 CE1 PHE A 53 -11.608 28.270 -16.693 1.00107.16 C ANISOU 389 CE1 PHE A 53 11585 18769 10362 1278 1588 -62 C ATOM 390 CE2 PHE A 53 -12.677 26.608 -15.311 1.00 66.10 C ANISOU 390 CE2 PHE A 53 6672 13184 5261 1584 1265 -218 C ATOM 391 CZ PHE A 53 -12.030 27.830 -15.444 1.00 67.02 C ANISOU 391 CZ PHE A 53 6570 13469 5425 1353 1393 -116 C ATOM 392 N ARG A 54 -14.630 23.853 -21.028 1.00 87.72 N ANISOU 392 N ARG A 54 10286 16051 6992 2019 1474 -441 N ATOM 393 CA ARG A 54 -14.709 23.015 -22.235 1.00 88.57 C ANISOU 393 CA ARG A 54 10548 16260 6846 2168 1538 -560 C ATOM 394 C ARG A 54 -15.826 23.447 -23.205 1.00 86.43 C ANISOU 394 C ARG A 54 10474 15943 6423 2029 1491 -468 C ATOM 395 O ARG A 54 -15.623 23.389 -24.416 1.00 87.91 O ANISOU 395 O ARG A 54 10711 16323 6370 2065 1611 -476 O ATOM 396 CB ARG A 54 -14.862 21.521 -21.868 1.00 89.59 C ANISOU 396 CB ARG A 54 10845 16225 6971 2407 1438 -779 C ATOM 397 CG ARG A 54 -13.827 20.967 -20.867 1.00 92.63 C ANISOU 397 CG ARG A 54 11062 16654 7477 2607 1470 -875 C ATOM 398 CD ARG A 54 -12.396 20.849 -21.419 1.00 97.86 C ANISOU 398 CD ARG A 54 11543 17651 7990 2780 1681 -948 C ATOM 399 NE ARG A 54 -12.293 19.810 -22.453 1.00104.62 N ANISOU 399 NE ARG A 54 12605 18527 8617 2981 1732 -1120 N ATOM 400 CZ ARG A 54 -11.212 19.559 -23.212 1.00110.87 C ANISOU 400 CZ ARG A 54 13299 19561 9264 3212 1899 -1243 C ATOM 401 NH1 ARG A 54 -10.086 20.274 -23.078 1.00114.01 N1+ ANISOU 401 NH1 ARG A 54 13374 20197 9748 3255 2016 -1205 N1+ ATOM 402 NH2 ARG A 54 -11.261 18.574 -24.118 1.00112.40 N1+ ANISOU 402 NH2 ARG A 54 13717 19680 9310 3348 1910 -1390 N1+ ATOM 403 N MET A 55 -16.965 23.882 -22.649 1.00 83.64 N ANISOU 403 N MET A 55 10229 15358 6194 1882 1319 -383 N ATOM 404 CA MET A 55 -18.110 24.438 -23.364 1.00 84.73 C ANISOU 404 CA MET A 55 10533 15465 6195 1766 1251 -289 C ATOM 405 C MET A 55 -17.914 25.944 -23.604 1.00 85.22 C ANISOU 405 C MET A 55 10495 15669 6216 1597 1378 -51 C ATOM 406 O MET A 55 -17.254 26.615 -22.809 1.00 86.65 O ANISOU 406 O MET A 55 10476 15933 6516 1522 1504 39 O ATOM 407 CB MET A 55 -19.384 24.199 -22.526 1.00 86.31 C ANISOU 407 CB MET A 55 10857 15387 6550 1678 1029 -283 C ATOM 408 CG MET A 55 -19.770 22.717 -22.350 1.00 91.59 C ANISOU 408 CG MET A 55 11645 15869 7285 1808 911 -500 C ATOM 409 SD MET A 55 -20.411 21.903 -23.838 1.00101.46 S ANISOU 409 SD MET A 55 13142 17148 8259 1930 874 -717 S ATOM 410 CE MET A 55 -22.099 22.565 -23.862 1.00102.17 C ANISOU 410 CE MET A 55 13341 17206 8274 1741 720 -596 C ATOM 411 N THR A 56 -18.538 26.444 -24.682 1.00 84.55 N ANISOU 411 N THR A 56 10559 15613 5954 1535 1345 48 N ATOM 412 CA THR A 56 -18.582 27.859 -25.060 1.00 83.29 C ANISOU 412 CA THR A 56 10369 15536 5742 1379 1451 297 C ATOM 413 C THR A 56 -19.323 28.714 -24.011 1.00 80.55 C ANISOU 413 C THR A 56 10032 14958 5617 1228 1317 448 C ATOM 414 O THR A 56 -20.327 28.260 -23.461 1.00 79.66 O ANISOU 414 O THR A 56 10031 14675 5563 1242 1116 393 O ATOM 415 CB THR A 56 -19.319 28.024 -26.419 1.00 85.01 C ANISOU 415 CB THR A 56 10758 15904 5639 1415 1475 346 C ATOM 416 CG2 THR A 56 -19.492 29.467 -26.935 1.00 83.71 C ANISOU 416 CG2 THR A 56 10610 15777 5420 1265 1570 631 C ATOM 417 OG1 THR A 56 -18.620 27.294 -27.409 1.00 89.37 O ANISOU 417 OG1 THR A 56 11292 16690 5974 1549 1637 216 O ATOM 418 N ARG A 57 -18.822 29.940 -23.772 1.00 79.20 N ANISOU 418 N ARG A 57 9741 14784 5569 1076 1438 630 N ATOM 419 CA ARG A 57 -19.432 30.919 -22.871 1.00 76.96 C ANISOU 419 CA ARG A 57 9462 14275 5506 935 1337 769 C ATOM 420 C ARG A 57 -20.764 31.441 -23.442 1.00 76.33 C ANISOU 420 C ARG A 57 9571 14109 5321 926 1205 891 C ATOM 421 O ARG A 57 -20.762 32.247 -24.372 1.00 77.94 O ANISOU 421 O ARG A 57 9859 14406 5350 890 1300 1067 O ATOM 422 CB ARG A 57 -18.424 32.053 -22.577 1.00 78.05 C ANISOU 422 CB ARG A 57 9466 14432 5756 756 1517 941 C ATOM 423 CG ARG A 57 -18.931 33.089 -21.550 1.00 77.70 C ANISOU 423 CG ARG A 57 9449 14141 5931 613 1428 1083 C ATOM 424 CD ARG A 57 -17.962 34.256 -21.317 1.00 80.26 C ANISOU 424 CD ARG A 57 9681 14469 6347 413 1621 1251 C ATOM 425 NE ARG A 57 -17.908 35.155 -22.479 1.00 84.72 N ANISOU 425 NE ARG A 57 10335 15171 6683 367 1804 1419 N ATOM 426 CZ ARG A 57 -17.226 36.311 -22.547 1.00 87.20 C ANISOU 426 CZ ARG A 57 10606 15503 7024 178 2013 1581 C ATOM 427 NH1 ARG A 57 -16.516 36.764 -21.504 1.00 86.97 N1+ ANISOU 427 NH1 ARG A 57 10431 15371 7241 10 2056 1579 N1+ ATOM 428 NH2 ARG A 57 -17.261 37.026 -23.678 1.00 89.71 N1+ ANISOU 428 NH2 ARG A 57 11035 15939 7113 147 2185 1742 N1+ ATOM 429 N THR A 58 -21.863 30.953 -22.856 1.00 75.94 N ANISOU 429 N THR A 58 9587 13894 5372 963 990 800 N ATOM 430 CA THR A 58 -23.241 31.340 -23.144 1.00 74.01 C ANISOU 430 CA THR A 58 9478 13566 5078 954 836 901 C ATOM 431 C THR A 58 -23.970 31.543 -21.803 1.00 71.53 C ANISOU 431 C THR A 58 9122 13008 5048 874 712 930 C ATOM 432 O THR A 58 -23.447 31.155 -20.758 1.00 69.84 O ANISOU 432 O THR A 58 8793 12698 5045 830 736 861 O ATOM 433 CB THR A 58 -23.986 30.237 -23.955 1.00 74.59 C ANISOU 433 CB THR A 58 9669 13717 4956 1073 689 731 C ATOM 434 CG2 THR A 58 -23.274 29.829 -25.254 1.00 75.27 C ANISOU 434 CG2 THR A 58 9808 14050 4740 1160 819 694 C ATOM 435 OG1 THR A 58 -24.255 29.073 -23.193 1.00 74.57 O ANISOU 435 OG1 THR A 58 9638 13602 5091 1114 590 502 O ATOM 436 N VAL A 59 -25.176 32.132 -21.851 1.00 71.62 N ANISOU 436 N VAL A 59 9222 12937 5054 866 576 1032 N ATOM 437 CA VAL A 59 -26.021 32.354 -20.673 1.00 67.38 C ANISOU 437 CA VAL A 59 8652 12180 4770 805 454 1046 C ATOM 438 C VAL A 59 -26.391 31.043 -19.943 1.00 67.46 C ANISOU 438 C VAL A 59 8628 12108 4897 836 334 809 C ATOM 439 O VAL A 59 -26.337 31.013 -18.717 1.00 68.93 O ANISOU 439 O VAL A 59 8745 12127 5316 778 303 778 O ATOM 440 CB VAL A 59 -27.324 33.121 -21.041 1.00 60.84 C ANISOU 440 CB VAL A 59 7915 11317 3885 827 326 1183 C ATOM 441 CG1 VAL A 59 -28.290 33.333 -19.855 1.00 58.68 C ANISOU 441 CG1 VAL A 59 7599 10831 3865 777 202 1175 C ATOM 442 CG2 VAL A 59 -26.992 34.473 -21.694 1.00 62.60 C ANISOU 442 CG2 VAL A 59 8204 11578 4002 808 460 1442 C ATOM 443 N THR A 60 -26.689 29.980 -20.711 1.00 67.82 N ANISOU 443 N THR A 60 8737 12259 4773 924 274 638 N ATOM 444 CA THR A 60 -27.022 28.643 -20.214 1.00 64.59 C ANISOU 444 CA THR A 60 8338 11746 4457 951 172 413 C ATOM 445 C THR A 60 -25.867 27.968 -19.440 1.00 63.88 C ANISOU 445 C THR A 60 8163 11613 4497 973 279 330 C ATOM 446 O THR A 60 -26.110 27.430 -18.360 1.00 61.46 O ANISOU 446 O THR A 60 7824 11138 4392 948 221 264 O ATOM 447 CB THR A 60 -27.435 27.712 -21.387 1.00 64.86 C ANISOU 447 CB THR A 60 8482 11898 4262 1031 102 241 C ATOM 448 CG2 THR A 60 -27.808 26.269 -21.000 1.00 62.55 C ANISOU 448 CG2 THR A 60 8238 11458 4072 1037 -1 16 C ATOM 449 OG1 THR A 60 -28.536 28.280 -22.073 1.00 67.38 O ANISOU 449 OG1 THR A 60 8859 12303 4439 1020 -9 322 O ATOM 450 N THR A 61 -24.639 28.034 -19.986 1.00 67.97 N ANISOU 450 N THR A 61 8636 12298 4893 1027 437 333 N ATOM 451 CA THR A 61 -23.435 27.472 -19.365 1.00 70.13 C ANISOU 451 CA THR A 61 8799 12577 5271 1073 535 248 C ATOM 452 C THR A 61 -22.933 28.306 -18.164 1.00 71.24 C ANISOU 452 C THR A 61 8807 12617 5643 961 570 369 C ATOM 453 O THR A 61 -22.372 27.718 -17.241 1.00 72.77 O ANISOU 453 O THR A 61 8913 12755 5979 990 575 284 O ATOM 454 CB THR A 61 -22.274 27.314 -20.385 1.00 69.32 C ANISOU 454 CB THR A 61 8649 12711 4978 1153 710 229 C ATOM 455 CG2 THR A 61 -22.615 26.439 -21.600 1.00 69.78 C ANISOU 455 CG2 THR A 61 8851 12862 4798 1274 676 79 C ATOM 456 OG1 THR A 61 -21.741 28.546 -20.834 1.00 69.67 O ANISOU 456 OG1 THR A 61 8652 12865 4954 1052 829 437 O ATOM 457 N ILE A 62 -23.187 29.628 -18.167 1.00 67.31 N ANISOU 457 N ILE A 62 8305 12092 5178 840 593 564 N ATOM 458 CA ILE A 62 -22.921 30.548 -17.055 1.00 65.22 C ANISOU 458 CA ILE A 62 7942 11703 5135 716 618 665 C ATOM 459 C ILE A 62 -23.820 30.276 -15.833 1.00 66.47 C ANISOU 459 C ILE A 62 8129 11650 5478 707 456 594 C ATOM 460 O ILE A 62 -23.320 30.314 -14.709 1.00 69.25 O ANISOU 460 O ILE A 62 8390 11918 6005 671 456 559 O ATOM 461 CB ILE A 62 -23.050 32.037 -17.511 1.00 64.25 C ANISOU 461 CB ILE A 62 7851 11569 4992 600 690 891 C ATOM 462 CG1 ILE A 62 -21.806 32.440 -18.335 1.00 65.53 C ANISOU 462 CG1 ILE A 62 7961 11929 5009 569 894 973 C ATOM 463 CG2 ILE A 62 -23.308 33.086 -16.401 1.00 64.00 C ANISOU 463 CG2 ILE A 62 7767 11352 5198 469 679 978 C ATOM 464 CD1 ILE A 62 -22.007 33.691 -19.203 1.00 68.56 C ANISOU 464 CD1 ILE A 62 8418 12284 5349 459 988 1208 C ATOM 465 N CYS A 63 -25.107 29.974 -16.076 1.00 64.96 N ANISOU 465 N CYS A 63 8055 11385 5240 734 319 565 N ATOM 466 CA CYS A 63 -26.087 29.605 -15.050 1.00 63.07 C ANISOU 466 CA CYS A 63 7845 10954 5166 712 181 496 C ATOM 467 C CYS A 63 -25.698 28.314 -14.309 1.00 62.09 C ANISOU 467 C CYS A 63 7719 10780 5091 791 157 311 C ATOM 468 O CYS A 63 -25.809 28.266 -13.084 1.00 62.07 O ANISOU 468 O CYS A 63 7681 10640 5262 764 121 284 O ATOM 469 CB CYS A 63 -27.502 29.448 -15.634 1.00 64.55 C ANISOU 469 CB CYS A 63 8135 11118 5275 716 47 487 C ATOM 470 SG CYS A 63 -28.188 31.041 -16.148 1.00 66.94 S ANISOU 470 SG CYS A 63 8456 11456 5522 669 46 720 S ATOM 471 N TYR A 64 -25.226 27.311 -15.069 1.00 63.15 N ANISOU 471 N TYR A 64 7909 11020 5065 902 180 182 N ATOM 472 CA TYR A 64 -24.779 26.014 -14.560 1.00 63.38 C ANISOU 472 CA TYR A 64 7972 10982 5126 1009 164 10 C ATOM 473 C TYR A 64 -23.419 26.083 -13.849 1.00 59.79 C ANISOU 473 C TYR A 64 7374 10572 4771 1049 255 22 C ATOM 474 O TYR A 64 -23.218 25.333 -12.894 1.00 60.57 O ANISOU 474 O TYR A 64 7476 10553 4984 1101 212 -55 O ATOM 475 CB TYR A 64 -24.734 25.001 -15.721 1.00 70.02 C ANISOU 475 CB TYR A 64 8918 11924 5763 1130 185 -135 C ATOM 476 CG TYR A 64 -26.045 24.715 -16.449 1.00 74.83 C ANISOU 476 CG TYR A 64 9670 12494 6270 1089 72 -198 C ATOM 477 CD1 TYR A 64 -27.308 25.046 -15.902 1.00 75.16 C ANISOU 477 CD1 TYR A 64 9734 12397 6427 972 -49 -157 C ATOM 478 CD2 TYR A 64 -25.988 24.098 -17.714 1.00 79.23 C ANISOU 478 CD2 TYR A 64 10325 13171 6606 1165 86 -312 C ATOM 479 CE1 TYR A 64 -28.488 24.800 -16.630 1.00 79.71 C ANISOU 479 CE1 TYR A 64 10406 12972 6907 926 -159 -228 C ATOM 480 CE2 TYR A 64 -27.167 23.840 -18.437 1.00 82.11 C ANISOU 480 CE2 TYR A 64 10804 13526 6867 1114 -28 -389 C ATOM 481 CZ TYR A 64 -28.416 24.206 -17.904 1.00 84.22 C ANISOU 481 CZ TYR A 64 11070 13672 7257 990 -154 -347 C ATOM 482 OH TYR A 64 -29.554 23.983 -18.624 1.00 88.54 O ANISOU 482 OH TYR A 64 11698 14245 7699 931 -275 -437 O ATOM 483 N LEU A 65 -22.530 26.988 -14.298 1.00 59.15 N ANISOU 483 N LEU A 65 7164 10671 4638 1022 383 116 N ATOM 484 CA LEU A 65 -21.236 27.262 -13.676 1.00 61.40 C ANISOU 484 CA LEU A 65 7275 11040 5016 1036 468 119 C ATOM 485 C LEU A 65 -21.394 27.876 -12.274 1.00 64.48 C ANISOU 485 C LEU A 65 7607 11277 5614 918 406 186 C ATOM 486 O LEU A 65 -20.762 27.382 -11.345 1.00 67.18 O ANISOU 486 O LEU A 65 7877 11594 6056 975 382 118 O ATOM 487 CB LEU A 65 -20.380 28.134 -14.628 1.00 63.00 C ANISOU 487 CB LEU A 65 7346 11468 5124 982 631 212 C ATOM 488 CG LEU A 65 -18.985 28.552 -14.104 1.00 65.18 C ANISOU 488 CG LEU A 65 7400 11871 5493 956 727 213 C ATOM 489 CD1 LEU A 65 -18.104 27.333 -13.764 1.00 65.86 C ANISOU 489 CD1 LEU A 65 7422 12059 5543 1169 733 45 C ATOM 490 CD2 LEU A 65 -18.292 29.517 -15.090 1.00 68.52 C ANISOU 490 CD2 LEU A 65 7705 12485 5842 833 901 330 C ATOM 491 N ASN A 66 -22.257 28.901 -12.138 1.00 62.87 N ANISOU 491 N ASN A 66 7440 10978 5469 769 379 318 N ATOM 492 CA ASN A 66 -22.570 29.566 -10.866 1.00 59.19 C ANISOU 492 CA ASN A 66 6942 10352 5194 660 322 372 C ATOM 493 C ASN A 66 -23.331 28.656 -9.887 1.00 56.67 C ANISOU 493 C ASN A 66 6714 9863 4953 729 194 263 C ATOM 494 O ASN A 66 -23.035 28.714 -8.694 1.00 58.11 O ANISOU 494 O ASN A 66 6841 9979 5260 724 165 235 O ATOM 495 CB ASN A 66 -23.343 30.874 -11.146 1.00 59.68 C ANISOU 495 CB ASN A 66 7061 10327 5289 526 315 526 C ATOM 496 CG ASN A 66 -22.424 32.037 -11.534 1.00 62.08 C ANISOU 496 CG ASN A 66 7266 10704 5617 396 449 658 C ATOM 497 ND2 ASN A 66 -22.090 32.166 -12.819 1.00 66.90 N ANISOU 497 ND2 ASN A 66 7873 11472 6074 400 560 720 N ATOM 498 OD1 ASN A 66 -22.026 32.820 -10.675 1.00 58.58 O ANISOU 498 OD1 ASN A 66 6761 10172 5324 284 462 699 O ATOM 499 N LEU A 67 -24.248 27.808 -10.391 1.00 55.22 N ANISOU 499 N LEU A 67 6678 9614 4692 786 120 197 N ATOM 500 CA LEU A 67 -24.931 26.769 -9.610 1.00 53.64 C ANISOU 500 CA LEU A 67 6586 9239 4557 832 20 92 C ATOM 501 C LEU A 67 -23.937 25.764 -9.004 1.00 53.96 C ANISOU 501 C LEU A 67 6619 9299 4584 987 41 -25 C ATOM 502 O LEU A 67 -23.984 25.527 -7.798 1.00 53.24 O ANISOU 502 O LEU A 67 6560 9076 4591 1016 -12 -64 O ATOM 503 CB LEU A 67 -26.010 26.083 -10.484 1.00 50.19 C ANISOU 503 CB LEU A 67 6297 8746 4026 834 -51 28 C ATOM 504 CG LEU A 67 -26.731 24.864 -9.853 1.00 48.31 C ANISOU 504 CG LEU A 67 6197 8318 3840 855 -134 -93 C ATOM 505 CD1 LEU A 67 -27.437 25.218 -8.531 1.00 48.43 C ANISOU 505 CD1 LEU A 67 6190 8180 4031 759 -183 -34 C ATOM 506 CD2 LEU A 67 -27.695 24.207 -10.862 1.00 47.86 C ANISOU 506 CD2 LEU A 67 6263 8240 3681 822 -198 -173 C ATOM 507 N ALA A 68 -23.036 25.232 -9.846 1.00 55.22 N ANISOU 507 N ALA A 68 6742 9629 4612 1104 120 -79 N ATOM 508 CA ALA A 68 -22.000 24.287 -9.442 1.00 56.36 C ANISOU 508 CA ALA A 68 6869 9813 4733 1291 144 -187 C ATOM 509 C ALA A 68 -20.925 24.884 -8.527 1.00 55.73 C ANISOU 509 C ALA A 68 6602 9811 4763 1285 165 -142 C ATOM 510 O ALA A 68 -20.436 24.154 -7.673 1.00 56.80 O ANISOU 510 O ALA A 68 6748 9892 4941 1412 124 -207 O ATOM 511 CB ALA A 68 -21.371 23.659 -10.683 1.00 57.66 C ANISOU 511 CB ALA A 68 7019 10166 4724 1426 238 -258 C ATOM 512 N LEU A 69 -20.603 26.182 -8.673 1.00 56.78 N ANISOU 512 N LEU A 69 6572 10068 4934 1137 229 -34 N ATOM 513 CA LEU A 69 -19.711 26.913 -7.766 1.00 60.74 C ANISOU 513 CA LEU A 69 6884 10656 5538 1092 247 -8 C ATOM 514 C LEU A 69 -20.292 27.045 -6.348 1.00 63.63 C ANISOU 514 C LEU A 69 7312 10821 6044 1037 139 3 C ATOM 515 O LEU A 69 -19.517 26.967 -5.396 1.00 64.62 O ANISOU 515 O LEU A 69 7347 10984 6223 1101 107 -37 O ATOM 516 CB LEU A 69 -19.368 28.303 -8.346 1.00 61.87 C ANISOU 516 CB LEU A 69 6877 10932 5698 903 350 103 C ATOM 517 CG LEU A 69 -18.281 28.282 -9.442 1.00 67.55 C ANISOU 517 CG LEU A 69 7457 11916 6293 945 490 92 C ATOM 518 CD1 LEU A 69 -18.276 29.602 -10.230 1.00 70.21 C ANISOU 518 CD1 LEU A 69 7707 12324 6644 723 602 227 C ATOM 519 CD2 LEU A 69 -16.881 27.965 -8.876 1.00 67.63 C ANISOU 519 CD2 LEU A 69 7273 12119 6306 1082 512 -9 C ATOM 520 N ALA A 70 -21.627 27.188 -6.230 1.00 62.08 N ANISOU 520 N ALA A 70 7260 10430 5896 926 82 56 N ATOM 521 CA ALA A 70 -22.338 27.175 -4.952 1.00 58.93 C ANISOU 521 CA ALA A 70 6928 9842 5620 873 -6 64 C ATOM 522 C ALA A 70 -22.292 25.788 -4.298 1.00 61.36 C ANISOU 522 C ALA A 70 7367 10042 5906 1044 -71 -37 C ATOM 523 O ALA A 70 -21.779 25.655 -3.190 1.00 63.05 O ANISOU 523 O ALA A 70 7558 10221 6178 1092 -115 -56 O ATOM 524 CB ALA A 70 -23.784 27.677 -5.127 1.00 59.13 C ANISOU 524 CB ALA A 70 7060 9712 5695 730 -42 138 C ATOM 525 N ASP A 71 -22.774 24.775 -5.032 1.00 64.00 N ANISOU 525 N ASP A 71 7854 10315 6147 1137 -77 -104 N ATOM 526 CA ASP A 71 -22.823 23.370 -4.624 1.00 66.50 C ANISOU 526 CA ASP A 71 8339 10488 6439 1293 -121 -197 C ATOM 527 C ASP A 71 -21.455 22.759 -4.264 1.00 66.92 C ANISOU 527 C ASP A 71 8310 10674 6443 1511 -98 -253 C ATOM 528 O ASP A 71 -21.370 22.060 -3.258 1.00 68.42 O ANISOU 528 O ASP A 71 8598 10752 6645 1642 -144 -290 O ATOM 529 CB ASP A 71 -23.545 22.507 -5.675 1.00 72.08 C ANISOU 529 CB ASP A 71 9234 11099 7053 1323 -121 -275 C ATOM 530 CG ASP A 71 -24.967 22.961 -6.013 1.00 78.36 C ANISOU 530 CG ASP A 71 10131 11737 7903 1137 -173 -247 C ATOM 531 OD1 ASP A 71 -25.669 23.437 -5.092 1.00 79.69 O ANISOU 531 OD1 ASP A 71 10287 11805 8189 1033 -212 -186 O ATOM 532 OD2 ASP A 71 -25.372 22.733 -7.171 1.00 80.54 O1- ANISOU 532 OD2 ASP A 71 10492 12008 8100 1099 -176 -294 O1- ATOM 533 N PHE A 72 -20.407 23.063 -5.048 1.00 65.51 N ANISOU 533 N PHE A 72 7949 10742 6200 1560 -24 -257 N ATOM 534 CA PHE A 72 -19.021 22.659 -4.793 1.00 67.86 C ANISOU 534 CA PHE A 72 8124 11211 6450 1778 -3 -316 C ATOM 535 C PHE A 72 -18.459 23.259 -3.491 1.00 67.11 C ANISOU 535 C PHE A 72 7869 11180 6447 1743 -53 -277 C ATOM 536 O PHE A 72 -17.867 22.522 -2.702 1.00 66.43 O ANISOU 536 O PHE A 72 7787 11110 6344 1940 -101 -323 O ATOM 537 CB PHE A 72 -18.148 23.011 -6.020 1.00 68.10 C ANISOU 537 CB PHE A 72 7975 11514 6387 1818 105 -335 C ATOM 538 CG PHE A 72 -16.667 22.687 -5.925 1.00 69.36 C ANISOU 538 CG PHE A 72 7986 11883 6483 2069 134 -411 C ATOM 539 CD1 PHE A 72 -16.206 21.392 -6.243 1.00 71.33 C ANISOU 539 CD1 PHE A 72 8374 12103 6624 2337 152 -512 C ATOM 540 CD2 PHE A 72 -15.761 23.623 -5.380 1.00 69.75 C ANISOU 540 CD2 PHE A 72 7756 12165 6581 2040 143 -391 C ATOM 541 CE1 PHE A 72 -14.867 21.070 -6.067 1.00 72.53 C ANISOU 541 CE1 PHE A 72 8382 12461 6714 2604 178 -581 C ATOM 542 CE2 PHE A 72 -14.427 23.279 -5.209 1.00 70.60 C ANISOU 542 CE2 PHE A 72 7694 12504 6626 2284 160 -468 C ATOM 543 CZ PHE A 72 -13.982 22.010 -5.555 1.00 71.60 C ANISOU 543 CZ PHE A 72 7955 12606 6643 2582 178 -558 C ATOM 544 N SER A 73 -18.676 24.572 -3.292 1.00 66.96 N ANISOU 544 N SER A 73 7723 11200 6519 1502 -44 -196 N ATOM 545 CA SER A 73 -18.223 25.321 -2.116 1.00 67.90 C ANISOU 545 CA SER A 73 7697 11380 6722 1439 -92 -177 C ATOM 546 C SER A 73 -18.917 24.884 -0.815 1.00 67.18 C ANISOU 546 C SER A 73 7789 11062 6674 1492 -193 -179 C ATOM 547 O SER A 73 -18.255 24.848 0.221 1.00 66.49 O ANISOU 547 O SER A 73 7636 11039 6588 1597 -253 -204 O ATOM 548 CB SER A 73 -18.415 26.832 -2.342 1.00 67.18 C ANISOU 548 CB SER A 73 7485 11319 6722 1157 -49 -94 C ATOM 549 OG SER A 73 -17.468 27.319 -3.270 1.00 68.86 O ANISOU 549 OG SER A 73 7537 11740 6888 1095 61 -79 O ATOM 550 N PHE A 74 -20.211 24.535 -0.895 1.00 65.37 N ANISOU 550 N PHE A 74 7784 10583 6469 1418 -211 -154 N ATOM 551 CA PHE A 74 -20.950 23.948 0.221 1.00 64.51 C ANISOU 551 CA PHE A 74 7864 10250 6396 1446 -284 -152 C ATOM 552 C PHE A 74 -20.448 22.540 0.597 1.00 65.24 C ANISOU 552 C PHE A 74 8097 10293 6400 1721 -310 -216 C ATOM 553 O PHE A 74 -20.010 22.335 1.734 1.00 68.64 O ANISOU 553 O PHE A 74 8548 10708 6823 1838 -368 -216 O ATOM 554 CB PHE A 74 -22.485 24.037 0.014 1.00 64.69 C ANISOU 554 CB PHE A 74 8067 10047 6466 1286 -284 -120 C ATOM 555 CG PHE A 74 -23.285 23.135 0.938 1.00 67.03 C ANISOU 555 CG PHE A 74 8600 10102 6767 1338 -327 -139 C ATOM 556 CD1 PHE A 74 -23.304 23.392 2.325 1.00 67.65 C ANISOU 556 CD1 PHE A 74 8701 10099 6902 1299 -373 -105 C ATOM 557 CD2 PHE A 74 -23.822 21.922 0.456 1.00 68.84 C ANISOU 557 CD2 PHE A 74 9040 10181 6935 1417 -313 -196 C ATOM 558 CE1 PHE A 74 -23.827 22.452 3.199 1.00 69.15 C ANISOU 558 CE1 PHE A 74 9121 10065 7087 1339 -394 -111 C ATOM 559 CE2 PHE A 74 -24.345 20.997 1.345 1.00 71.02 C ANISOU 559 CE2 PHE A 74 9549 10219 7216 1440 -333 -210 C ATOM 560 CZ PHE A 74 -24.333 21.257 2.711 1.00 70.77 C ANISOU 560 CZ PHE A 74 9538 10111 7239 1403 -369 -160 C ATOM 561 N THR A 75 -20.506 21.598 -0.360 1.00 63.60 N ANISOU 561 N THR A 75 8003 10051 6111 1840 -266 -271 N ATOM 562 CA THR A 75 -20.209 20.180 -0.115 1.00 64.06 C ANISOU 562 CA THR A 75 8240 10018 6082 2115 -275 -334 C ATOM 563 C THR A 75 -18.748 19.904 0.300 1.00 63.70 C ANISOU 563 C THR A 75 8017 10206 5981 2356 -295 -357 C ATOM 564 O THR A 75 -18.510 18.879 0.935 1.00 65.82 O ANISOU 564 O THR A 75 8430 10392 6188 2606 -328 -381 O ATOM 565 CB THR A 75 -20.560 19.278 -1.328 1.00 64.91 C ANISOU 565 CB THR A 75 8490 10066 6108 2186 -213 -408 C ATOM 566 CG2 THR A 75 -22.060 19.287 -1.666 1.00 61.29 C ANISOU 566 CG2 THR A 75 8242 9357 5687 1981 -215 -407 C ATOM 567 OG1 THR A 75 -19.808 19.629 -2.476 1.00 66.81 O ANISOU 567 OG1 THR A 75 8510 10564 6311 2152 -152 -418 O ATOM 568 N ALA A 76 -17.824 20.840 0.018 1.00 61.41 N ANISOU 568 N ALA A 76 7417 10209 5707 2288 -274 -350 N ATOM 569 CA ALA A 76 -16.444 20.831 0.506 1.00 63.21 C ANISOU 569 CA ALA A 76 7425 10705 5885 2495 -301 -384 C ATOM 570 C ALA A 76 -16.299 21.039 2.031 1.00 65.01 C ANISOU 570 C ALA A 76 7641 10916 6145 2515 -405 -351 C ATOM 571 O ALA A 76 -15.263 20.655 2.573 1.00 69.02 O ANISOU 571 O ALA A 76 8028 11610 6588 2750 -457 -384 O ATOM 572 CB ALA A 76 -15.646 21.894 -0.263 1.00 62.97 C ANISOU 572 CB ALA A 76 7059 10999 5870 2367 -236 -392 C ATOM 573 N THR A 77 -17.319 21.616 2.696 1.00 62.50 N ANISOU 573 N THR A 77 7437 10396 5913 2288 -437 -292 N ATOM 574 CA THR A 77 -17.344 21.832 4.149 1.00 63.17 C ANISOU 574 CA THR A 77 7534 10453 6016 2290 -528 -263 C ATOM 575 C THR A 77 -17.945 20.653 4.946 1.00 63.89 C ANISOU 575 C THR A 77 7953 10269 6054 2464 -568 -241 C ATOM 576 O THR A 77 -17.834 20.663 6.171 1.00 66.39 O ANISOU 576 O THR A 77 8309 10567 6351 2519 -644 -213 O ATOM 577 CB THR A 77 -18.127 23.114 4.547 1.00 62.80 C ANISOU 577 CB THR A 77 7439 10338 6086 1956 -529 -213 C ATOM 578 CG2 THR A 77 -17.706 24.374 3.786 1.00 63.15 C ANISOU 578 CG2 THR A 77 7239 10569 6187 1752 -459 -216 C ATOM 579 OG1 THR A 77 -19.536 22.970 4.487 1.00 62.47 O ANISOU 579 OG1 THR A 77 7662 9984 6088 1839 -505 -172 O ATOM 580 N LEU A 78 -18.550 19.660 4.271 1.00 63.24 N ANISOU 580 N LEU A 78 8117 9971 5942 2541 -512 -255 N ATOM 581 CA LEU A 78 -19.128 18.466 4.896 1.00 66.65 C ANISOU 581 CA LEU A 78 8896 10097 6333 2659 -525 -232 C ATOM 582 C LEU A 78 -18.190 17.583 5.759 1.00 73.02 C ANISOU 582 C LEU A 78 9767 10948 7030 2997 -590 -223 C ATOM 583 O LEU A 78 -18.704 17.055 6.743 1.00 74.51 O ANISOU 583 O LEU A 78 10191 10923 7197 3029 -620 -168 O ATOM 584 CB LEU A 78 -19.890 17.616 3.859 1.00 66.24 C ANISOU 584 CB LEU A 78 9081 9829 6260 2677 -446 -276 C ATOM 585 CG LEU A 78 -21.162 18.288 3.300 1.00 63.88 C ANISOU 585 CG LEU A 78 8783 9438 6051 2353 -398 -276 C ATOM 586 CD1 LEU A 78 -21.709 17.508 2.097 1.00 65.87 C ANISOU 586 CD1 LEU A 78 9273 9494 6261 2378 -335 -342 C ATOM 587 CD2 LEU A 78 -22.258 18.496 4.363 1.00 61.84 C ANISOU 587 CD2 LEU A 78 8598 9018 5880 2119 -424 -211 C ATOM 588 N PRO A 79 -16.857 17.510 5.502 1.00 76.05 N ANISOU 588 N PRO A 79 9963 11597 7334 3264 -612 -269 N ATOM 589 CA PRO A 79 -15.894 16.926 6.465 1.00 78.05 C ANISOU 589 CA PRO A 79 10269 11913 7473 3608 -693 -250 C ATOM 590 C PRO A 79 -15.761 17.628 7.834 1.00 77.81 C ANISOU 590 C PRO A 79 10135 11982 7447 3527 -795 -201 C ATOM 591 O PRO A 79 -15.299 16.983 8.775 1.00 78.78 O ANISOU 591 O PRO A 79 10443 12014 7476 3745 -859 -151 O ATOM 592 CB PRO A 79 -14.553 16.890 5.706 1.00 80.47 C ANISOU 592 CB PRO A 79 10294 12569 7713 3860 -695 -324 C ATOM 593 CG PRO A 79 -14.732 17.842 4.536 1.00 80.40 C ANISOU 593 CG PRO A 79 10024 12729 7795 3575 -624 -367 C ATOM 594 CD PRO A 79 -16.204 17.671 4.202 1.00 77.28 C ANISOU 594 CD PRO A 79 9881 12000 7480 3305 -555 -340 C ATOM 595 N PHE A 80 -16.184 18.899 7.941 1.00 76.58 N ANISOU 595 N PHE A 80 9709 12001 7386 3225 -808 -212 N ATOM 596 CA PHE A 80 -16.212 19.658 9.195 1.00 75.70 C ANISOU 596 CA PHE A 80 9517 11970 7277 3125 -900 -183 C ATOM 597 C PHE A 80 -17.561 19.511 9.923 1.00 74.42 C ANISOU 597 C PHE A 80 9667 11458 7150 2962 -881 -110 C ATOM 598 O PHE A 80 -17.580 19.549 11.154 1.00 78.68 O ANISOU 598 O PHE A 80 10278 11983 7634 3000 -954 -71 O ATOM 599 CB PHE A 80 -15.916 21.147 8.918 1.00 74.69 C ANISOU 599 CB PHE A 80 9028 12108 7243 2841 -904 -229 C ATOM 600 CG PHE A 80 -14.548 21.434 8.322 1.00 78.81 C ANISOU 600 CG PHE A 80 9203 13014 7727 2967 -918 -306 C ATOM 601 CD1 PHE A 80 -14.325 21.286 6.936 1.00 80.34 C ANISOU 601 CD1 PHE A 80 9299 13273 7953 2944 -817 -340 C ATOM 602 CD2 PHE A 80 -13.450 21.717 9.162 1.00 80.82 C ANISOU 602 CD2 PHE A 80 9218 13586 7904 3104 -1030 -349 C ATOM 603 CE1 PHE A 80 -13.054 21.476 6.411 1.00 83.38 C ANISOU 603 CE1 PHE A 80 9353 14027 8302 3051 -811 -413 C ATOM 604 CE2 PHE A 80 -12.187 21.906 8.619 1.00 84.01 C ANISOU 604 CE2 PHE A 80 9271 14374 8276 3208 -1037 -431 C ATOM 605 CZ PHE A 80 -11.991 21.790 7.249 1.00 85.22 C ANISOU 605 CZ PHE A 80 9328 14582 8469 3179 -919 -460 C ATOM 606 N LEU A 81 -18.647 19.337 9.158 1.00 70.43 N ANISOU 606 N LEU A 81 9343 10690 6728 2781 -783 -96 N ATOM 607 CA LEU A 81 -19.997 19.181 9.695 1.00 67.97 C ANISOU 607 CA LEU A 81 9305 10065 6456 2611 -750 -37 C ATOM 608 C LEU A 81 -20.216 17.758 10.238 1.00 71.42 C ANISOU 608 C LEU A 81 10116 10224 6796 2833 -728 7 C ATOM 609 O LEU A 81 -20.689 17.612 11.366 1.00 74.18 O ANISOU 609 O LEU A 81 10695 10348 7143 2742 -711 66 O ATOM 610 CB LEU A 81 -21.051 19.550 8.622 1.00 62.06 C ANISOU 610 CB LEU A 81 8565 9179 5837 2306 -663 -47 C ATOM 611 CG LEU A 81 -20.894 20.964 8.006 1.00 58.76 C ANISOU 611 CG LEU A 81 7831 8978 5519 2074 -659 -73 C ATOM 612 CD1 LEU A 81 -21.981 21.243 6.947 1.00 59.66 C ANISOU 612 CD1 LEU A 81 7999 8932 5737 1816 -582 -65 C ATOM 613 CD2 LEU A 81 -20.827 22.081 9.066 1.00 55.01 C ANISOU 613 CD2 LEU A 81 7207 8630 5066 1963 -723 -60 C ATOM 614 N ILE A 82 -19.804 16.740 9.462 1.00 73.08 N ANISOU 614 N ILE A 82 10407 10436 6923 3122 -716 -20 N ATOM 615 CA ILE A 82 -19.990 15.316 9.769 1.00 78.72 C ANISOU 615 CA ILE A 82 11523 10837 7551 3325 -675 22 C ATOM 616 C ILE A 82 -19.377 14.899 11.123 1.00 79.49 C ANISOU 616 C ILE A 82 11713 10980 7507 3623 -762 90 C ATOM 617 O ILE A 82 -20.018 14.146 11.854 1.00 78.39 O ANISOU 617 O ILE A 82 11915 10561 7308 3670 -734 168 O ATOM 618 CB ILE A 82 -19.422 14.402 8.634 1.00 83.35 C ANISOU 618 CB ILE A 82 12208 11354 8107 3511 -610 -44 C ATOM 619 CG1 ILE A 82 -19.900 12.935 8.745 1.00 87.37 C ANISOU 619 CG1 ILE A 82 13180 11480 8538 3684 -546 -6 C ATOM 620 CG2 ILE A 82 -17.886 14.458 8.505 1.00 85.53 C ANISOU 620 CG2 ILE A 82 12216 11974 8307 3814 -671 -91 C ATOM 621 CD1 ILE A 82 -19.449 12.035 7.584 1.00 90.48 C ANISOU 621 CD1 ILE A 82 13707 11791 8879 3921 -484 -79 C ATOM 622 N VAL A 83 -18.181 15.425 11.447 1.00 81.09 N ANISOU 622 N VAL A 83 11618 11548 7646 3823 -867 63 N ATOM 623 CA VAL A 83 -17.473 15.139 12.695 1.00 80.21 C ANISOU 623 CA VAL A 83 11561 11533 7384 4108 -974 125 C ATOM 624 C VAL A 83 -18.052 15.904 13.900 1.00 75.55 C ANISOU 624 C VAL A 83 10936 10962 6807 3874 -1024 170 C ATOM 625 O VAL A 83 -17.987 15.379 15.009 1.00 76.32 O ANISOU 625 O VAL A 83 11195 11032 6770 4057 -1090 244 O ATOM 626 CB VAL A 83 -15.952 15.445 12.595 1.00 81.09 C ANISOU 626 CB VAL A 83 11332 12067 7411 4404 -1081 67 C ATOM 627 CG1 VAL A 83 -15.265 14.558 11.543 1.00 82.23 C ANISOU 627 CG1 VAL A 83 11391 12266 7585 4528 -1009 -10 C ATOM 628 CG2 VAL A 83 -15.596 16.926 12.370 1.00 78.64 C ANISOU 628 CG2 VAL A 83 10604 12121 7155 4179 -1168 12 C ATOM 629 N SER A 84 -18.655 17.081 13.687 1.00 72.05 N ANISOU 629 N SER A 84 10301 10563 6511 3489 -992 128 N ATOM 630 CA SER A 84 -19.321 17.797 14.770 1.00 72.10 C ANISOU 630 CA SER A 84 10319 10535 6540 3252 -1014 163 C ATOM 631 C SER A 84 -20.667 17.124 15.106 1.00 76.16 C ANISOU 631 C SER A 84 11219 10645 7075 3120 -908 240 C ATOM 632 O SER A 84 -20.935 16.837 16.274 1.00 79.91 O ANISOU 632 O SER A 84 11859 11028 7474 3110 -923 306 O ATOM 633 CB SER A 84 -19.426 19.294 14.423 1.00 71.36 C ANISOU 633 CB SER A 84 9897 10619 6597 2910 -1009 92 C ATOM 634 OG SER A 84 -19.937 20.037 15.512 1.00 69.81 O ANISOU 634 OG SER A 84 9730 10368 6429 2685 -1016 115 O ATOM 635 N MET A 85 -21.439 16.772 14.065 1.00 76.39 N ANISOU 635 N MET A 85 11389 10441 7194 3010 -796 225 N ATOM 636 CA MET A 85 -22.700 16.034 14.174 1.00 77.75 C ANISOU 636 CA MET A 85 11921 10236 7384 2876 -685 282 C ATOM 637 C MET A 85 -22.541 14.674 14.875 1.00 81.33 C ANISOU 637 C MET A 85 12743 10483 7676 3181 -675 368 C ATOM 638 O MET A 85 -23.417 14.283 15.643 1.00 82.05 O ANISOU 638 O MET A 85 13116 10334 7727 3105 -614 447 O ATOM 639 CB MET A 85 -23.320 15.861 12.774 1.00 80.48 C ANISOU 639 CB MET A 85 12312 10415 7851 2694 -582 225 C ATOM 640 CG MET A 85 -23.872 17.175 12.206 1.00 82.00 C ANISOU 640 CG MET A 85 12284 10672 8203 2327 -553 182 C ATOM 641 SD MET A 85 -24.304 17.144 10.443 1.00 84.61 S ANISOU 641 SD MET A 85 12636 10871 8639 2158 -462 107 S ATOM 642 CE MET A 85 -25.818 16.145 10.467 1.00 87.53 C ANISOU 642 CE MET A 85 13483 10831 8944 2220 -360 136 C ATOM 643 N ALA A 86 -21.407 14.006 14.639 1.00 83.75 N ANISOU 643 N ALA A 86 13061 10876 7884 3537 -724 358 N ATOM 644 CA ALA A 86 -21.030 12.716 15.228 1.00 83.09 C ANISOU 644 CA ALA A 86 13342 10595 7635 3879 -717 449 C ATOM 645 C ALA A 86 -20.776 12.758 16.746 1.00 82.14 C ANISOU 645 C ALA A 86 13229 10620 7361 4052 -825 535 C ATOM 646 O ALA A 86 -21.002 11.749 17.414 1.00 85.67 O ANISOU 646 O ALA A 86 14025 10869 7655 4309 -812 640 O ATOM 647 CB ALA A 86 -19.789 12.172 14.504 1.00 84.55 C ANISOU 647 CB ALA A 86 13518 10853 7755 4243 -740 407 C ATOM 648 N MET A 87 -20.331 13.917 17.258 1.00 77.14 N ANISOU 648 N MET A 87 12237 10319 6755 3920 -929 491 N ATOM 649 CA MET A 87 -20.083 14.167 18.680 1.00 78.13 C ANISOU 649 CA MET A 87 12337 10621 6728 4053 -1045 548 C ATOM 650 C MET A 87 -21.338 14.662 19.434 1.00 77.07 C ANISOU 650 C MET A 87 12293 10359 6629 3726 -992 586 C ATOM 651 O MET A 87 -21.236 14.935 20.630 1.00 79.10 O ANISOU 651 O MET A 87 12434 10825 6795 3733 -1091 593 O ATOM 652 CB MET A 87 -18.926 15.180 18.816 1.00 78.67 C ANISOU 652 CB MET A 87 11943 11169 6779 4139 -1203 455 C ATOM 653 CG MET A 87 -17.578 14.700 18.250 1.00 83.63 C ANISOU 653 CG MET A 87 12486 11999 7293 4572 -1290 440 C ATOM 654 SD MET A 87 -16.342 16.014 18.044 1.00 85.93 S ANISOU 654 SD MET A 87 12182 12882 7584 4597 -1459 307 S ATOM 655 CE MET A 87 -15.849 16.291 19.766 1.00 86.01 C ANISOU 655 CE MET A 87 12165 13039 7475 4502 -1578 335 C ATOM 656 N GLY A 88 -22.467 14.789 18.722 1.00 74.84 N ANISOU 656 N GLY A 88 12208 9756 6471 3444 -838 600 N ATOM 657 CA GLY A 88 -23.708 15.353 19.240 1.00 74.84 C ANISOU 657 CA GLY A 88 12266 9651 6516 3131 -772 625 C ATOM 658 C GLY A 88 -23.630 16.878 19.221 1.00 72.91 C ANISOU 658 C GLY A 88 11630 9673 6399 2863 -827 527 C ATOM 659 O GLY A 88 -23.993 17.528 20.197 1.00 74.37 O ANISOU 659 O GLY A 88 11775 9943 6540 2756 -857 536 O ATOM 660 N GLU A 89 -23.122 17.430 18.112 1.00 70.80 N ANISOU 660 N GLU A 89 11089 9532 6279 2759 -833 434 N ATOM 661 CA GLU A 89 -23.025 18.854 17.779 1.00 70.57 C ANISOU 661 CA GLU A 89 10707 9716 6391 2495 -862 344 C ATOM 662 C GLU A 89 -21.906 19.594 18.531 1.00 67.02 C ANISOU 662 C GLU A 89 9978 9624 5861 2592 -1010 293 C ATOM 663 O GLU A 89 -21.781 20.811 18.375 1.00 61.97 O ANISOU 663 O GLU A 89 9084 9140 5321 2359 -1030 221 O ATOM 664 CB GLU A 89 -24.393 19.578 17.874 1.00 75.00 C ANISOU 664 CB GLU A 89 11330 10110 7054 2163 -764 354 C ATOM 665 CG GLU A 89 -25.590 18.871 17.193 1.00 79.91 C ANISOU 665 CG GLU A 89 12203 10404 7755 2029 -618 390 C ATOM 666 CD GLU A 89 -25.367 18.513 15.724 1.00 84.38 C ANISOU 666 CD GLU A 89 12683 10954 8425 2019 -592 336 C ATOM 667 OE1 GLU A 89 -24.669 19.280 15.027 1.00 85.15 O ANISOU 667 OE1 GLU A 89 12493 11220 8641 1873 -614 269 O ATOM 668 OE2 GLU A 89 -25.902 17.464 15.309 1.00 87.03 O1- ANISOU 668 OE2 GLU A 89 13255 11100 8713 2159 -543 361 O1- ATOM 669 N LYS A 90 -21.070 18.873 19.297 1.00 71.49 N ANISOU 669 N LYS A 90 10585 10329 6248 2928 -1116 322 N ATOM 670 CA LYS A 90 -19.822 19.427 19.838 1.00 73.69 C ANISOU 670 CA LYS A 90 10555 10996 6447 3021 -1270 249 C ATOM 671 C LYS A 90 -18.863 19.755 18.680 1.00 73.98 C ANISOU 671 C LYS A 90 10241 11279 6591 3005 -1300 150 C ATOM 672 O LYS A 90 -18.542 18.857 17.904 1.00 75.07 O ANISOU 672 O LYS A 90 10415 11307 6801 3052 -1226 154 O ATOM 673 CB LYS A 90 -19.122 18.436 20.794 1.00 75.72 C ANISOU 673 CB LYS A 90 10943 11362 6466 3416 -1388 311 C ATOM 674 CG LYS A 90 -19.945 17.908 21.980 1.00 76.49 C ANISOU 674 CG LYS A 90 11422 11218 6425 3467 -1351 429 C ATOM 675 CD LYS A 90 -19.069 17.067 22.931 1.00 82.56 C ANISOU 675 CD LYS A 90 12269 12165 6934 3865 -1496 486 C ATOM 676 CE LYS A 90 -19.846 16.233 23.963 1.00 87.25 C ANISOU 676 CE LYS A 90 13351 12422 7376 4027 -1418 647 C ATOM 677 NZ LYS A 90 -20.264 14.929 23.419 1.00 89.21 N1+ ANISOU 677 NZ LYS A 90 13872 12351 7672 4159 -1296 717 N1+ ATOM 678 N TRP A 91 -18.422 21.011 18.611 1.00 74.24 N ANISOU 678 N TRP A 91 9934 11649 6624 2925 -1401 54 N ATOM 679 CA TRP A 91 -17.576 21.538 17.547 1.00 74.54 C ANISOU 679 CA TRP A 91 9613 11949 6761 2866 -1417 -44 C ATOM 680 C TRP A 91 -16.101 21.419 17.977 1.00 76.87 C ANISOU 680 C TRP A 91 9662 12637 6907 3145 -1572 -103 C ATOM 681 O TRP A 91 -15.725 22.100 18.933 1.00 76.84 O ANISOU 681 O TRP A 91 9445 12897 6852 3062 -1678 -180 O ATOM 682 CB TRP A 91 -17.988 23.002 17.308 1.00 75.24 C ANISOU 682 CB TRP A 91 9487 12089 7010 2468 -1375 -121 C ATOM 683 CG TRP A 91 -17.244 23.698 16.210 1.00 78.98 C ANISOU 683 CG TRP A 91 9659 12745 7606 2356 -1340 -195 C ATOM 684 CD1 TRP A 91 -16.199 24.534 16.382 1.00 82.33 C ANISOU 684 CD1 TRP A 91 9723 13520 8037 2284 -1408 -302 C ATOM 685 CD2 TRP A 91 -17.423 23.571 14.768 1.00 80.36 C ANISOU 685 CD2 TRP A 91 9868 12767 7900 2292 -1220 -171 C ATOM 686 CE2 TRP A 91 -16.437 24.373 14.116 1.00 82.15 C ANISOU 686 CE2 TRP A 91 9757 13262 8195 2193 -1214 -252 C ATOM 687 CE3 TRP A 91 -18.321 22.858 13.941 1.00 80.10 C ANISOU 687 CE3 TRP A 91 10116 12406 7913 2297 -1116 -95 C ATOM 688 NE1 TRP A 91 -15.733 24.953 15.154 1.00 83.49 N ANISOU 688 NE1 TRP A 91 9687 13734 8303 2179 -1325 -333 N ATOM 689 CZ2 TRP A 91 -16.337 24.440 12.715 1.00 81.71 C ANISOU 689 CZ2 TRP A 91 9650 13156 8239 2119 -1108 -249 C ATOM 690 CZ3 TRP A 91 -18.243 22.933 12.536 1.00 80.27 C ANISOU 690 CZ3 TRP A 91 10075 12389 8036 2221 -1026 -107 C ATOM 691 CH2 TRP A 91 -17.252 23.723 11.924 1.00 80.28 C ANISOU 691 CH2 TRP A 91 9750 12661 8090 2143 -1023 -177 C ATOM 692 N PRO A 92 -15.303 20.550 17.314 1.00 79.21 N ANISOU 692 N PRO A 92 9971 12998 7125 3482 -1591 -81 N ATOM 693 CA PRO A 92 -13.907 20.329 17.734 1.00 81.24 C ANISOU 693 CA PRO A 92 9965 13668 7237 3781 -1744 -141 C ATOM 694 C PRO A 92 -12.896 21.385 17.239 1.00 82.57 C ANISOU 694 C PRO A 92 9664 14210 7500 3617 -1766 -279 C ATOM 695 O PRO A 92 -11.790 21.430 17.778 1.00 86.26 O ANISOU 695 O PRO A 92 9841 15078 7856 3800 -1900 -356 O ATOM 696 CB PRO A 92 -13.596 18.936 17.168 1.00 83.19 C ANISOU 696 CB PRO A 92 10420 13799 7388 4195 -1724 -66 C ATOM 697 CG PRO A 92 -14.400 18.871 15.880 1.00 81.87 C ANISOU 697 CG PRO A 92 10436 13287 7384 4013 -1548 -36 C ATOM 698 CD PRO A 92 -15.672 19.642 16.221 1.00 80.26 C ANISOU 698 CD PRO A 92 10366 12834 7295 3615 -1475 -11 C ATOM 699 N PHE A 93 -13.269 22.196 16.232 1.00 82.21 N ANISOU 699 N PHE A 93 9532 14057 7646 3281 -1637 -311 N ATOM 700 CA PHE A 93 -12.394 23.195 15.607 1.00 78.92 C ANISOU 700 CA PHE A 93 8703 13960 7324 3097 -1625 -427 C ATOM 701 C PHE A 93 -12.433 24.539 16.367 1.00 85.27 C ANISOU 701 C PHE A 93 9316 14904 8178 2756 -1672 -513 C ATOM 702 O PHE A 93 -13.184 24.691 17.331 1.00 88.96 O ANISOU 702 O PHE A 93 9973 15220 8607 2672 -1710 -484 O ATOM 703 CB PHE A 93 -12.793 23.378 14.125 1.00 69.66 C ANISOU 703 CB PHE A 93 7557 12601 6311 2929 -1458 -407 C ATOM 704 CG PHE A 93 -12.898 22.105 13.305 1.00 65.29 C ANISOU 704 CG PHE A 93 7287 11804 5716 3208 -1395 -326 C ATOM 705 CD1 PHE A 93 -11.734 21.466 12.829 1.00 63.77 C ANISOU 705 CD1 PHE A 93 7008 11808 5414 3583 -1435 -345 C ATOM 706 CD2 PHE A 93 -14.147 21.470 13.137 1.00 58.84 C ANISOU 706 CD2 PHE A 93 6823 10565 4967 3096 -1293 -240 C ATOM 707 CE1 PHE A 93 -11.835 20.258 12.152 1.00 63.78 C ANISOU 707 CE1 PHE A 93 7300 11560 5376 3840 -1368 -282 C ATOM 708 CE2 PHE A 93 -14.226 20.264 12.457 1.00 59.13 C ANISOU 708 CE2 PHE A 93 7133 10367 4966 3324 -1230 -183 C ATOM 709 CZ PHE A 93 -13.076 19.663 11.962 1.00 62.40 C ANISOU 709 CZ PHE A 93 7488 10950 5272 3696 -1264 -204 C ATOM 710 N GLY A 94 -11.602 25.494 15.915 1.00 87.01 N ANISOU 710 N GLY A 94 9167 15413 8480 2550 -1658 -624 N ATOM 711 CA GLY A 94 -11.446 26.813 16.530 1.00 89.95 C ANISOU 711 CA GLY A 94 9343 15938 8894 2228 -1702 -729 C ATOM 712 C GLY A 94 -12.613 27.766 16.213 1.00 90.09 C ANISOU 712 C GLY A 94 9550 15608 9070 1862 -1580 -692 C ATOM 713 O GLY A 94 -13.502 27.458 15.417 1.00 90.66 O ANISOU 713 O GLY A 94 9857 15354 9235 1825 -1457 -592 O ATOM 714 N TRP A 95 -12.565 28.949 16.851 1.00 87.00 N ANISOU 714 N TRP A 95 9052 15300 8702 1592 -1620 -786 N ATOM 715 CA TRP A 95 -13.510 30.063 16.705 1.00 83.52 C ANISOU 715 CA TRP A 95 8740 14573 8420 1235 -1500 -772 C ATOM 716 C TRP A 95 -13.588 30.638 15.279 1.00 82.56 C ANISOU 716 C TRP A 95 8499 14404 8466 1027 -1349 -761 C ATOM 717 O TRP A 95 -14.683 30.969 14.822 1.00 80.39 O ANISOU 717 O TRP A 95 8409 13817 8317 852 -1227 -687 O ATOM 718 CB TRP A 95 -13.147 31.155 17.734 1.00 86.93 C ANISOU 718 CB TRP A 95 9057 15136 8838 993 -1570 -901 C ATOM 719 CG TRP A 95 -13.976 32.408 17.718 1.00 89.51 C ANISOU 719 CG TRP A 95 9400 15265 9345 598 -1438 -930 C ATOM 720 CD1 TRP A 95 -15.136 32.581 18.388 1.00 89.18 C ANISOU 720 CD1 TRP A 95 9625 14887 9373 451 -1367 -880 C ATOM 721 CD2 TRP A 95 -13.773 33.635 16.948 1.00 92.39 C ANISOU 721 CD2 TRP A 95 9513 15754 9836 310 -1354 -1011 C ATOM 722 CE2 TRP A 95 -14.848 34.531 17.237 1.00 91.14 C ANISOU 722 CE2 TRP A 95 9511 15299 9821 14 -1236 -997 C ATOM 723 CE3 TRP A 95 -12.791 34.086 16.034 1.00 95.18 C ANISOU 723 CE3 TRP A 95 9527 16441 10195 276 -1356 -1093 C ATOM 724 NE1 TRP A 95 -15.646 33.833 18.118 1.00 89.10 N ANISOU 724 NE1 TRP A 95 9554 14774 9524 116 -1250 -921 N ATOM 725 CZ2 TRP A 95 -14.935 35.812 16.661 1.00 91.11 C ANISOU 725 CZ2 TRP A 95 9366 15293 9958 -310 -1120 -1051 C ATOM 726 CZ3 TRP A 95 -12.874 35.363 15.442 1.00 95.26 C ANISOU 726 CZ3 TRP A 95 9383 16462 10348 -72 -1232 -1150 C ATOM 727 CH2 TRP A 95 -13.941 36.227 15.756 1.00 93.23 C ANISOU 727 CH2 TRP A 95 9319 15878 10227 -359 -1115 -1123 C ATOM 728 N PHE A 96 -12.427 30.732 14.609 1.00 84.63 N ANISOU 728 N PHE A 96 8447 14987 8721 1054 -1354 -832 N ATOM 729 CA PHE A 96 -12.300 31.180 13.224 1.00 82.98 C ANISOU 729 CA PHE A 96 8124 14760 8647 868 -1203 -815 C ATOM 730 C PHE A 96 -13.025 30.254 12.233 1.00 79.27 C ANISOU 730 C PHE A 96 7882 14038 8199 1043 -1113 -682 C ATOM 731 O PHE A 96 -13.756 30.750 11.377 1.00 77.95 O ANISOU 731 O PHE A 96 7820 13645 8153 856 -982 -617 O ATOM 732 CB PHE A 96 -10.805 31.386 12.891 1.00 84.48 C ANISOU 732 CB PHE A 96 7911 15384 8802 873 -1224 -928 C ATOM 733 CG PHE A 96 -10.470 31.701 11.443 1.00 84.43 C ANISOU 733 CG PHE A 96 7783 15392 8905 717 -1058 -904 C ATOM 734 CD1 PHE A 96 -10.663 33.005 10.940 1.00 84.46 C ANISOU 734 CD1 PHE A 96 7748 15297 9047 326 -935 -919 C ATOM 735 CD2 PHE A 96 -10.107 30.669 10.550 1.00 86.63 C ANISOU 735 CD2 PHE A 96 8001 15780 9135 970 -1019 -864 C ATOM 736 CE1 PHE A 96 -10.425 33.274 9.598 1.00 85.78 C ANISOU 736 CE1 PHE A 96 7822 15475 9294 188 -775 -881 C ATOM 737 CE2 PHE A 96 -9.876 30.958 9.212 1.00 86.85 C ANISOU 737 CE2 PHE A 96 7924 15835 9242 830 -861 -841 C ATOM 738 CZ PHE A 96 -10.023 32.257 8.742 1.00 86.40 C ANISOU 738 CZ PHE A 96 7831 15683 9314 437 -739 -843 C ATOM 739 N LEU A 97 -12.838 28.934 12.406 1.00 77.48 N ANISOU 739 N LEU A 97 7746 13843 7850 1406 -1184 -644 N ATOM 740 CA LEU A 97 -13.473 27.892 11.601 1.00 73.28 C ANISOU 740 CA LEU A 97 7450 13063 7330 1567 -1102 -538 C ATOM 741 C LEU A 97 -14.978 27.750 11.878 1.00 72.96 C ANISOU 741 C LEU A 97 7760 12617 7343 1479 -1063 -445 C ATOM 742 O LEU A 97 -15.710 27.463 10.933 1.00 75.55 O ANISOU 742 O LEU A 97 8254 12714 7739 1446 -962 -373 O ATOM 743 CB LEU A 97 -12.731 26.551 11.801 1.00 73.44 C ANISOU 743 CB LEU A 97 7499 13202 7203 1984 -1180 -530 C ATOM 744 CG LEU A 97 -11.320 26.517 11.171 1.00 74.38 C ANISOU 744 CG LEU A 97 7267 13724 7269 2125 -1196 -615 C ATOM 745 CD1 LEU A 97 -10.570 25.234 11.570 1.00 75.81 C ANISOU 745 CD1 LEU A 97 7533 13966 7306 2579 -1261 -592 C ATOM 746 CD2 LEU A 97 -11.352 26.683 9.635 1.00 72.63 C ANISOU 746 CD2 LEU A 97 6916 13520 7158 1925 -1041 -617 C ATOM 747 N CYS A 98 -15.424 27.979 13.122 1.00 72.06 N ANISOU 747 N CYS A 98 7755 12433 7192 1441 -1139 -452 N ATOM 748 CA CYS A 98 -16.849 28.011 13.488 1.00 73.21 C ANISOU 748 CA CYS A 98 8204 12221 7392 1334 -1089 -374 C ATOM 749 C CYS A 98 -17.623 29.041 12.645 1.00 72.20 C ANISOU 749 C CYS A 98 8062 11942 7430 1015 -969 -359 C ATOM 750 O CYS A 98 -18.584 28.682 11.963 1.00 71.14 O ANISOU 750 O CYS A 98 8144 11524 7361 955 -894 -281 O ATOM 751 CB CYS A 98 -16.988 28.224 15.016 1.00 76.55 C ANISOU 751 CB CYS A 98 8714 12639 7731 1341 -1184 -398 C ATOM 752 SG CYS A 98 -18.596 28.682 15.737 1.00 79.68 S ANISOU 752 SG CYS A 98 9364 12689 8222 1092 -1108 -351 S ATOM 753 N LYS A 99 -17.131 30.288 12.628 1.00 71.35 N ANISOU 753 N LYS A 99 7702 12022 7387 809 -945 -431 N ATOM 754 CA LYS A 99 -17.754 31.370 11.876 1.00 66.36 C ANISOU 754 CA LYS A 99 7065 11245 6902 527 -823 -404 C ATOM 755 C LYS A 99 -17.598 31.196 10.357 1.00 64.79 C ANISOU 755 C LYS A 99 6779 11094 6743 533 -729 -364 C ATOM 756 O LYS A 99 -18.591 31.354 9.654 1.00 64.28 O ANISOU 756 O LYS A 99 6818 10835 6771 401 -630 -293 O ATOM 757 CB LYS A 99 -17.216 32.724 12.372 1.00 66.74 C ANISOU 757 CB LYS A 99 6934 11420 7004 264 -824 -499 C ATOM 758 CG LYS A 99 -17.607 33.002 13.836 1.00 68.02 C ANISOU 758 CG LYS A 99 7184 11542 7118 235 -911 -556 C ATOM 759 CD LYS A 99 -17.108 34.350 14.378 1.00 70.68 C ANISOU 759 CD LYS A 99 7360 11981 7513 -53 -901 -669 C ATOM 760 CE LYS A 99 -17.769 35.592 13.757 1.00 70.72 C ANISOU 760 CE LYS A 99 7506 11696 7668 -303 -772 -623 C ATOM 761 NZ LYS A 99 -19.218 35.629 14.016 1.00 69.65 N1+ ANISOU 761 NZ LYS A 99 7627 11307 7529 -272 -782 -586 N1+ ATOM 762 N LEU A 100 -16.387 30.847 9.883 1.00 62.89 N ANISOU 762 N LEU A 100 6349 11122 6424 697 -758 -409 N ATOM 763 CA LEU A 100 -16.052 30.714 8.460 1.00 61.55 C ANISOU 763 CA LEU A 100 6099 11014 6274 713 -659 -378 C ATOM 764 C LEU A 100 -16.863 29.634 7.723 1.00 59.88 C ANISOU 764 C LEU A 100 6140 10571 6040 886 -631 -293 C ATOM 765 O LEU A 100 -17.441 29.945 6.682 1.00 57.71 O ANISOU 765 O LEU A 100 5938 10165 5825 784 -534 -233 O ATOM 766 CB LEU A 100 -14.520 30.561 8.295 1.00 60.35 C ANISOU 766 CB LEU A 100 5661 11231 6037 859 -692 -461 C ATOM 767 CG LEU A 100 -14.002 30.394 6.840 1.00 59.62 C ANISOU 767 CG LEU A 100 5449 11261 5941 893 -581 -446 C ATOM 768 CD1 LEU A 100 -12.609 31.025 6.653 1.00 65.92 C ANISOU 768 CD1 LEU A 100 5877 12447 6721 824 -566 -545 C ATOM 769 CD2 LEU A 100 -14.006 28.926 6.361 1.00 58.04 C ANISOU 769 CD2 LEU A 100 5391 11017 5646 1232 -601 -418 C ATOM 770 N ILE A 101 -16.930 28.420 8.289 1.00 59.93 N ANISOU 770 N ILE A 101 6294 10524 5953 1145 -713 -290 N ATOM 771 CA ILE A 101 -17.662 27.310 7.684 1.00 56.12 C ANISOU 771 CA ILE A 101 6049 9837 5439 1312 -683 -232 C ATOM 772 C ILE A 101 -19.180 27.552 7.662 1.00 53.20 C ANISOU 772 C ILE A 101 5903 9154 5157 1137 -632 -163 C ATOM 773 O ILE A 101 -19.793 27.378 6.612 1.00 52.03 O ANISOU 773 O ILE A 101 5846 8885 5038 1105 -561 -124 O ATOM 774 CB ILE A 101 -17.286 25.942 8.332 1.00 54.85 C ANISOU 774 CB ILE A 101 6019 9669 5154 1625 -773 -240 C ATOM 775 CG1 ILE A 101 -15.895 25.499 7.820 1.00 58.80 C ANISOU 775 CG1 ILE A 101 6286 10494 5560 1851 -812 -306 C ATOM 776 CG2 ILE A 101 -18.306 24.794 8.164 1.00 52.17 C ANISOU 776 CG2 ILE A 101 5986 9041 4796 1741 -733 -185 C ATOM 777 CD1 ILE A 101 -15.057 24.754 8.858 1.00 63.25 C ANISOU 777 CD1 ILE A 101 6892 11146 5996 2139 -933 -323 C ATOM 778 N HIS A 102 -19.763 28.018 8.773 1.00 51.86 N ANISOU 778 N HIS A 102 5813 8869 5023 1025 -668 -153 N ATOM 779 CA HIS A 102 -21.203 28.278 8.830 1.00 56.60 C ANISOU 779 CA HIS A 102 6609 9194 5704 880 -620 -93 C ATOM 780 C HIS A 102 -21.653 29.474 7.963 1.00 56.90 C ANISOU 780 C HIS A 102 6559 9208 5855 642 -537 -66 C ATOM 781 O HIS A 102 -22.754 29.419 7.415 1.00 52.57 O ANISOU 781 O HIS A 102 6143 8465 5365 558 -489 -11 O ATOM 782 CB HIS A 102 -21.672 28.353 10.291 1.00 59.18 C ANISOU 782 CB HIS A 102 7049 9412 6023 846 -670 -94 C ATOM 783 CG HIS A 102 -21.639 27.029 11.030 1.00 62.72 C ANISOU 783 CG HIS A 102 7665 9812 6354 1079 -733 -88 C ATOM 784 CD2 HIS A 102 -21.434 25.738 10.592 1.00 64.39 C ANISOU 784 CD2 HIS A 102 8126 9806 6532 1181 -712 -41 C ATOM 785 ND1 HIS A 102 -21.861 26.910 12.391 1.00 66.25 N ANISOU 785 ND1 HIS A 102 8035 10444 6693 1240 -828 -130 N ATOM 786 CE1 HIS A 102 -21.784 25.616 12.709 1.00 67.12 C ANISOU 786 CE1 HIS A 102 8361 10440 6703 1451 -860 -94 C ATOM 787 NE2 HIS A 102 -21.541 24.844 11.658 1.00 66.11 N ANISOU 787 NE2 HIS A 102 8440 10055 6622 1405 -783 -42 N ATOM 788 N ILE A 103 -20.785 30.481 7.768 1.00 57.96 N ANISOU 788 N ILE A 103 6473 9536 6015 532 -515 -100 N ATOM 789 CA ILE A 103 -20.985 31.554 6.786 1.00 55.94 C ANISOU 789 CA ILE A 103 6157 9250 5848 332 -419 -57 C ATOM 790 C ILE A 103 -21.002 31.026 5.332 1.00 54.67 C ANISOU 790 C ILE A 103 5996 9125 5650 413 -363 -20 C ATOM 791 O ILE A 103 -21.922 31.358 4.583 1.00 54.31 O ANISOU 791 O ILE A 103 6038 8949 5648 332 -303 48 O ATOM 792 CB ILE A 103 -19.929 32.695 6.958 1.00 56.44 C ANISOU 792 CB ILE A 103 6005 9490 5949 158 -395 -109 C ATOM 793 CG1 ILE A 103 -20.255 33.547 8.208 1.00 56.25 C ANISOU 793 CG1 ILE A 103 6033 9349 5992 0 -416 -133 C ATOM 794 CG2 ILE A 103 -19.708 33.632 5.748 1.00 54.85 C ANISOU 794 CG2 ILE A 103 5720 9324 5798 11 -279 -58 C ATOM 795 CD1 ILE A 103 -19.065 34.373 8.725 1.00 57.93 C ANISOU 795 CD1 ILE A 103 6049 9724 6237 -191 -399 -211 C ATOM 796 N VAL A 104 -20.025 30.175 4.974 1.00 52.66 N ANISOU 796 N VAL A 104 5644 9060 5305 590 -383 -67 N ATOM 797 CA VAL A 104 -19.990 29.453 3.700 1.00 51.66 C ANISOU 797 CA VAL A 104 5533 8972 5124 693 -328 -50 C ATOM 798 C VAL A 104 -21.241 28.574 3.490 1.00 51.83 C ANISOU 798 C VAL A 104 5805 8760 5130 777 -343 -16 C ATOM 799 O VAL A 104 -21.805 28.607 2.400 1.00 50.27 O ANISOU 799 O VAL A 104 5666 8512 4921 755 -289 17 O ATOM 800 CB VAL A 104 -18.686 28.604 3.572 1.00 53.01 C ANISOU 800 CB VAL A 104 5552 9393 5195 900 -348 -121 C ATOM 801 CG1 VAL A 104 -18.679 27.502 2.489 1.00 47.38 C ANISOU 801 CG1 VAL A 104 4901 8694 4409 1046 -294 -119 C ATOM 802 CG2 VAL A 104 -17.468 29.520 3.352 1.00 55.31 C ANISOU 802 CG2 VAL A 104 5557 9952 5507 773 -311 -162 C ATOM 803 N VAL A 105 -21.669 27.835 4.519 1.00 53.33 N ANISOU 803 N VAL A 105 6145 8807 5310 859 -411 -28 N ATOM 804 CA VAL A 105 -22.854 26.990 4.438 1.00 54.38 C ANISOU 804 CA VAL A 105 6515 8711 5437 899 -414 -6 C ATOM 805 C VAL A 105 -24.148 27.800 4.187 1.00 57.59 C ANISOU 805 C VAL A 105 6971 8975 5936 694 -377 52 C ATOM 806 O VAL A 105 -24.860 27.464 3.243 1.00 59.17 O ANISOU 806 O VAL A 105 7252 9099 6130 674 -348 71 O ATOM 807 CB VAL A 105 -22.993 26.035 5.656 1.00 52.17 C ANISOU 807 CB VAL A 105 6393 8311 5119 1020 -477 -21 C ATOM 808 CG1 VAL A 105 -24.328 25.276 5.700 1.00 51.15 C ANISOU 808 CG1 VAL A 105 6496 7926 5013 974 -462 3 C ATOM 809 CG2 VAL A 105 -21.853 24.999 5.696 1.00 50.45 C ANISOU 809 CG2 VAL A 105 6181 8198 4789 1283 -512 -67 C ATOM 810 N ASP A 106 -24.401 28.884 4.945 1.00 59.29 N ANISOU 810 N ASP A 106 7136 9161 6231 550 -380 75 N ATOM 811 CA ASP A 106 -25.542 29.781 4.685 1.00 61.28 C ANISOU 811 CA ASP A 106 7441 9272 6572 389 -346 131 C ATOM 812 C ASP A 106 -25.534 30.359 3.254 1.00 62.41 C ANISOU 812 C ASP A 106 7503 9479 6730 309 -284 182 C ATOM 813 O ASP A 106 -26.507 30.144 2.525 1.00 60.76 O ANISOU 813 O ASP A 106 7368 9175 6541 265 -268 227 O ATOM 814 CB ASP A 106 -25.787 30.903 5.731 1.00 63.92 C ANISOU 814 CB ASP A 106 7744 9562 6980 270 -352 133 C ATOM 815 CG ASP A 106 -26.147 30.475 7.160 1.00 67.73 C ANISOU 815 CG ASP A 106 8371 9902 7462 303 -391 117 C ATOM 816 OD1 ASP A 106 -26.130 29.264 7.465 1.00 69.65 O ANISOU 816 OD1 ASP A 106 8687 10153 7623 447 -435 84 O ATOM 817 OD2 ASP A 106 -26.488 31.376 7.958 1.00 68.45 O1- ANISOU 817 OD2 ASP A 106 8511 9871 7626 193 -369 141 O1- ATOM 818 N ILE A 107 -24.427 31.003 2.849 1.00 62.73 N ANISOU 818 N ILE A 107 7389 9694 6752 288 -248 176 N ATOM 819 CA ILE A 107 -24.278 31.645 1.535 1.00 59.13 C ANISOU 819 CA ILE A 107 6871 9299 6298 204 -171 240 C ATOM 820 C ILE A 107 -24.533 30.697 0.350 1.00 57.58 C ANISOU 820 C ILE A 107 6744 9120 6013 311 -166 244 C ATOM 821 O ILE A 107 -25.239 31.060 -0.587 1.00 62.91 O ANISOU 821 O ILE A 107 7473 9743 6687 261 -141 307 O ATOM 822 CB ILE A 107 -22.875 32.319 1.344 1.00 60.05 C ANISOU 822 CB ILE A 107 6799 9610 6406 142 -116 223 C ATOM 823 CG1 ILE A 107 -22.786 33.578 2.221 1.00 62.02 C ANISOU 823 CG1 ILE A 107 6996 9815 6753 -29 -103 223 C ATOM 824 CG2 ILE A 107 -22.481 32.689 -0.111 1.00 60.57 C ANISOU 824 CG2 ILE A 107 6819 9767 6430 99 -24 286 C ATOM 825 CD1 ILE A 107 -21.376 34.164 2.385 1.00 65.66 C ANISOU 825 CD1 ILE A 107 7262 10467 7216 -139 -41 192 C ATOM 826 N ASN A 108 -23.953 29.501 0.408 1.00 50.96 N ANISOU 826 N ASN A 108 5915 8358 5091 472 -194 171 N ATOM 827 CA ASN A 108 -23.951 28.542 -0.694 1.00 48.53 C ANISOU 827 CA ASN A 108 5676 8076 4687 575 -180 152 C ATOM 828 C ASN A 108 -25.159 27.591 -0.677 1.00 51.14 C ANISOU 828 C ASN A 108 6193 8221 5018 592 -229 137 C ATOM 829 O ASN A 108 -25.379 26.950 -1.703 1.00 53.56 O ANISOU 829 O ASN A 108 6562 8525 5263 603 -220 133 O ATOM 830 CB ASN A 108 -22.608 27.788 -0.675 1.00 49.57 C ANISOU 830 CB ASN A 108 5753 8353 4728 757 -178 73 C ATOM 831 CG ASN A 108 -21.431 28.680 -1.091 1.00 51.65 C ANISOU 831 CG ASN A 108 5796 8848 4980 727 -117 76 C ATOM 832 ND2 ASN A 108 -20.532 28.996 -0.163 1.00 51.34 N ANISOU 832 ND2 ASN A 108 5641 8883 4984 719 -148 47 N ATOM 833 OD1 ASN A 108 -21.332 29.091 -2.242 1.00 56.18 O ANISOU 833 OD1 ASN A 108 6301 9545 5500 702 -40 101 O ATOM 834 N LEU A 109 -25.908 27.502 0.432 1.00 53.18 N ANISOU 834 N LEU A 109 6539 8334 5334 582 -277 121 N ATOM 835 CA LEU A 109 -27.224 26.859 0.435 1.00 54.65 C ANISOU 835 CA LEU A 109 6884 8349 5533 555 -306 106 C ATOM 836 C LEU A 109 -28.270 27.823 -0.143 1.00 54.92 C ANISOU 836 C LEU A 109 6894 8346 5629 411 -298 174 C ATOM 837 O LEU A 109 -29.041 27.415 -1.011 1.00 56.48 O ANISOU 837 O LEU A 109 7157 8504 5797 388 -313 162 O ATOM 838 CB LEU A 109 -27.622 26.379 1.847 1.00 52.00 C ANISOU 838 CB LEU A 109 6653 7874 5232 578 -341 80 C ATOM 839 CG LEU A 109 -26.872 25.119 2.336 1.00 51.70 C ANISOU 839 CG LEU A 109 6715 7817 5110 757 -357 16 C ATOM 840 CD1 LEU A 109 -27.262 24.802 3.788 1.00 51.19 C ANISOU 840 CD1 LEU A 109 6799 7584 5066 768 -381 10 C ATOM 841 CD2 LEU A 109 -27.063 23.889 1.425 1.00 50.88 C ANISOU 841 CD2 LEU A 109 6717 7690 4924 832 -342 -41 C ATOM 842 N PHE A 110 -28.222 29.101 0.273 1.00 51.55 N ANISOU 842 N PHE A 110 6374 7931 5282 319 -277 240 N ATOM 843 CA PHE A 110 -28.987 30.177 -0.365 1.00 52.02 C ANISOU 843 CA PHE A 110 6407 7969 5387 222 -259 320 C ATOM 844 C PHE A 110 -28.659 30.325 -1.856 1.00 52.33 C ANISOU 844 C PHE A 110 6406 8135 5342 242 -229 359 C ATOM 845 O PHE A 110 -29.570 30.362 -2.679 1.00 51.89 O ANISOU 845 O PHE A 110 6379 8076 5263 222 -243 399 O ATOM 846 CB PHE A 110 -28.779 31.518 0.355 1.00 51.95 C ANISOU 846 CB PHE A 110 6333 7928 5476 129 -227 376 C ATOM 847 CG PHE A 110 -29.578 31.734 1.623 1.00 47.96 C ANISOU 847 CG PHE A 110 5884 7279 5059 81 -249 368 C ATOM 848 CD1 PHE A 110 -30.983 31.589 1.628 1.00 45.17 C ANISOU 848 CD1 PHE A 110 5581 6849 4734 59 -266 388 C ATOM 849 CD2 PHE A 110 -28.929 32.208 2.781 1.00 47.35 C ANISOU 849 CD2 PHE A 110 5797 7167 5026 59 -251 334 C ATOM 850 CE1 PHE A 110 -31.703 31.865 2.781 1.00 45.27 C ANISOU 850 CE1 PHE A 110 5631 6745 4823 16 -271 376 C ATOM 851 CE2 PHE A 110 -29.665 32.469 3.922 1.00 46.96 C ANISOU 851 CE2 PHE A 110 5807 6993 5042 17 -259 325 C ATOM 852 CZ PHE A 110 -31.044 32.297 3.923 1.00 45.60 C ANISOU 852 CZ PHE A 110 5683 6740 4904 -4 -261 347 C ATOM 853 N GLY A 111 -27.356 30.335 -2.172 1.00 49.99 N ANISOU 853 N GLY A 111 6036 7971 4988 286 -186 347 N ATOM 854 CA GLY A 111 -26.800 30.350 -3.521 1.00 50.86 C ANISOU 854 CA GLY A 111 6114 8213 4997 309 -141 383 C ATOM 855 C GLY A 111 -27.411 29.231 -4.367 1.00 53.98 C ANISOU 855 C GLY A 111 6604 8620 5288 392 -182 318 C ATOM 856 O GLY A 111 -27.948 29.532 -5.425 1.00 57.51 O ANISOU 856 O GLY A 111 7069 9120 5662 382 -180 360 O ATOM 857 N SER A 112 -27.426 27.983 -3.869 1.00 53.69 N ANISOU 857 N SER A 112 6641 8525 5232 475 -219 214 N ATOM 858 CA SER A 112 -28.048 26.835 -4.533 1.00 54.13 C ANISOU 858 CA SER A 112 6811 8567 5190 539 -249 128 C ATOM 859 C SER A 112 -29.531 27.084 -4.887 1.00 52.46 C ANISOU 859 C SER A 112 6653 8289 4992 448 -301 142 C ATOM 860 O SER A 112 -29.868 27.085 -6.073 1.00 56.72 O ANISOU 860 O SER A 112 7220 8901 5428 456 -317 119 O ATOM 861 CB SER A 112 -27.842 25.560 -3.680 1.00 54.50 C ANISOU 861 CB SER A 112 6966 8509 5234 634 -271 25 C ATOM 862 OG SER A 112 -28.150 24.373 -4.390 1.00 52.81 O ANISOU 862 OG SER A 112 6890 8237 4937 667 -294 -70 O ATOM 863 N VAL A 113 -30.380 27.370 -3.885 1.00 51.28 N ANISOU 863 N VAL A 113 6505 8021 4959 366 -329 174 N ATOM 864 CA VAL A 113 -31.821 27.529 -4.106 1.00 54.46 C ANISOU 864 CA VAL A 113 6927 8385 5379 288 -380 178 C ATOM 865 C VAL A 113 -32.179 28.765 -4.965 1.00 53.99 C ANISOU 865 C VAL A 113 6782 8425 5307 263 -375 295 C ATOM 866 O VAL A 113 -33.060 28.675 -5.823 1.00 53.47 O ANISOU 866 O VAL A 113 6716 8419 5182 249 -424 294 O ATOM 867 CB VAL A 113 -32.640 27.540 -2.781 1.00 53.36 C ANISOU 867 CB VAL A 113 6818 8094 5362 218 -397 164 C ATOM 868 CG1 VAL A 113 -32.418 26.257 -1.958 1.00 52.12 C ANISOU 868 CG1 VAL A 113 6788 7823 5192 247 -398 57 C ATOM 869 CG2 VAL A 113 -32.434 28.770 -1.880 1.00 52.39 C ANISOU 869 CG2 VAL A 113 6625 7940 5342 197 -361 250 C ATOM 870 N PHE A 114 -31.454 29.879 -4.785 1.00 51.61 N ANISOU 870 N PHE A 114 6413 8143 5054 256 -317 395 N ATOM 871 CA PHE A 114 -31.649 31.093 -5.576 1.00 52.29 C ANISOU 871 CA PHE A 114 6453 8290 5123 241 -296 524 C ATOM 872 C PHE A 114 -31.165 30.928 -7.028 1.00 56.58 C ANISOU 872 C PHE A 114 7003 8989 5505 296 -281 541 C ATOM 873 O PHE A 114 -31.828 31.420 -7.940 1.00 57.05 O ANISOU 873 O PHE A 114 7064 9116 5496 309 -304 619 O ATOM 874 CB PHE A 114 -30.983 32.308 -4.893 1.00 51.93 C ANISOU 874 CB PHE A 114 6360 8201 5171 194 -219 616 C ATOM 875 CG PHE A 114 -31.485 32.699 -3.504 1.00 51.23 C ANISOU 875 CG PHE A 114 6271 7966 5227 139 -231 613 C ATOM 876 CD1 PHE A 114 -32.836 32.537 -3.121 1.00 50.89 C ANISOU 876 CD1 PHE A 114 6257 7853 5227 134 -295 570 C ATOM 877 CD2 PHE A 114 -30.618 33.392 -2.631 1.00 51.39 C ANISOU 877 CD2 PHE A 114 6260 7932 5335 83 -172 643 C ATOM 878 CE1 PHE A 114 -33.262 32.969 -1.873 1.00 51.93 C ANISOU 878 CE1 PHE A 114 6390 7861 5480 89 -291 566 C ATOM 879 CE2 PHE A 114 -31.067 33.825 -1.392 1.00 53.54 C ANISOU 879 CE2 PHE A 114 6543 8074 5725 37 -180 630 C ATOM 880 CZ PHE A 114 -32.379 33.598 -1.007 1.00 53.39 C ANISOU 880 CZ PHE A 114 6559 7985 5742 48 -235 596 C ATOM 881 N LEU A 115 -30.061 30.199 -7.242 1.00 57.02 N ANISOU 881 N LEU A 115 7063 9116 5486 344 -242 470 N ATOM 882 CA LEU A 115 -29.528 29.905 -8.577 1.00 50.41 C ANISOU 882 CA LEU A 115 6240 8435 4480 403 -218 468 C ATOM 883 C LEU A 115 -30.366 28.855 -9.329 1.00 51.33 C ANISOU 883 C LEU A 115 6430 8578 4494 431 -306 365 C ATOM 884 O LEU A 115 -30.419 28.926 -10.555 1.00 53.54 O ANISOU 884 O LEU A 115 6726 8989 4627 463 -318 387 O ATOM 885 CB LEU A 115 -28.034 29.522 -8.491 1.00 44.51 C ANISOU 885 CB LEU A 115 5461 7767 3683 461 -142 411 C ATOM 886 CG LEU A 115 -27.125 30.736 -8.165 1.00 44.49 C ANISOU 886 CG LEU A 115 5357 7789 3759 412 -48 496 C ATOM 887 CD1 LEU A 115 -25.748 30.305 -7.618 1.00 45.24 C ANISOU 887 CD1 LEU A 115 5388 8001 3799 485 15 417 C ATOM 888 CD2 LEU A 115 -27.009 31.711 -9.359 1.00 45.31 C ANISOU 888 CD2 LEU A 115 5441 7950 3825 352 19 651 C ATOM 889 N ILE A 116 -31.053 27.953 -8.603 1.00 51.09 N ANISOU 889 N ILE A 116 6453 8430 4530 408 -364 249 N ATOM 890 CA ILE A 116 -32.058 27.034 -9.153 1.00 52.97 C ANISOU 890 CA ILE A 116 6758 8681 4687 392 -445 135 C ATOM 891 C ILE A 116 -33.346 27.763 -9.594 1.00 57.60 C ANISOU 891 C ILE A 116 7290 9333 5261 349 -516 210 C ATOM 892 O ILE A 116 -33.896 27.421 -10.642 1.00 62.05 O ANISOU 892 O ILE A 116 7867 10025 5684 362 -574 171 O ATOM 893 CB ILE A 116 -32.400 25.888 -8.148 1.00 49.33 C ANISOU 893 CB ILE A 116 6377 8052 4312 351 -472 7 C ATOM 894 CG1 ILE A 116 -31.232 24.881 -8.076 1.00 48.17 C ANISOU 894 CG1 ILE A 116 6326 7871 4105 441 -424 -99 C ATOM 895 CG2 ILE A 116 -33.720 25.134 -8.424 1.00 51.01 C ANISOU 895 CG2 ILE A 116 6625 8258 4497 266 -556 -89 C ATOM 896 CD1 ILE A 116 -31.256 23.973 -6.836 1.00 45.45 C ANISOU 896 CD1 ILE A 116 6109 7340 3821 414 -439 -218 C ATOM 897 N GLY A 117 -33.776 28.772 -8.814 1.00 58.47 N ANISOU 897 N GLY A 117 7338 9368 5509 310 -515 313 N ATOM 898 CA GLY A 117 -34.912 29.635 -9.147 1.00 60.52 C ANISOU 898 CA GLY A 117 7539 9699 5758 310 -574 405 C ATOM 899 C GLY A 117 -34.569 30.565 -10.322 1.00 61.67 C ANISOU 899 C GLY A 117 7676 9978 5778 383 -543 544 C ATOM 900 O GLY A 117 -35.421 30.801 -11.175 1.00 63.12 O ANISOU 900 O GLY A 117 7836 10277 5869 423 -612 599 O ATOM 901 N PHE A 118 -33.314 31.043 -10.396 1.00 62.30 N ANISOU 901 N PHE A 118 7772 10055 5846 403 -438 606 N ATOM 902 CA PHE A 118 -32.785 31.852 -11.494 1.00 62.57 C ANISOU 902 CA PHE A 118 7817 10209 5748 455 -381 742 C ATOM 903 C PHE A 118 -32.682 31.069 -12.820 1.00 65.04 C ANISOU 903 C PHE A 118 8171 10695 5845 511 -417 664 C ATOM 904 O PHE A 118 -32.980 31.644 -13.864 1.00 65.83 O ANISOU 904 O PHE A 118 8288 10928 5797 566 -440 758 O ATOM 905 CB PHE A 118 -31.450 32.487 -11.051 1.00 66.22 C ANISOU 905 CB PHE A 118 8265 10631 6264 428 -244 811 C ATOM 906 CG PHE A 118 -30.759 33.383 -12.060 1.00 70.78 C ANISOU 906 CG PHE A 118 8863 11303 6727 451 -153 971 C ATOM 907 CD1 PHE A 118 -29.773 32.859 -12.922 1.00 73.22 C ANISOU 907 CD1 PHE A 118 9193 11773 6854 495 -101 950 C ATOM 908 CD2 PHE A 118 -31.204 34.709 -12.248 1.00 71.75 C ANISOU 908 CD2 PHE A 118 9002 11342 6918 430 -107 1144 C ATOM 909 CE1 PHE A 118 -29.221 33.666 -13.906 1.00 77.54 C ANISOU 909 CE1 PHE A 118 9771 12406 7284 506 0 1107 C ATOM 910 CE2 PHE A 118 -30.639 35.496 -13.242 1.00 76.03 C ANISOU 910 CE2 PHE A 118 9593 11947 7349 443 -6 1305 C ATOM 911 CZ PHE A 118 -29.652 34.973 -14.068 1.00 78.85 C ANISOU 911 CZ PHE A 118 9966 12475 7519 475 49 1290 C ATOM 912 N ILE A 119 -32.330 29.771 -12.750 1.00 65.43 N ANISOU 912 N ILE A 119 8253 10744 5863 508 -422 493 N ATOM 913 CA ILE A 119 -32.356 28.831 -13.879 1.00 58.32 C ANISOU 913 CA ILE A 119 7409 9992 4757 556 -456 385 C ATOM 914 C ILE A 119 -33.782 28.559 -14.396 1.00 55.42 C ANISOU 914 C ILE A 119 7041 9703 4315 541 -597 336 C ATOM 915 O ILE A 119 -33.962 28.462 -15.608 1.00 58.90 O ANISOU 915 O ILE A 119 7504 10320 4555 591 -640 340 O ATOM 916 CB ILE A 119 -31.643 27.484 -13.529 1.00 57.23 C ANISOU 916 CB ILE A 119 7330 9794 4623 566 -428 202 C ATOM 917 CG1 ILE A 119 -30.115 27.680 -13.547 1.00 58.93 C ANISOU 917 CG1 ILE A 119 7514 10008 4868 611 -294 249 C ATOM 918 CG2 ILE A 119 -31.994 26.265 -14.417 1.00 50.90 C ANISOU 918 CG2 ILE A 119 6609 9111 3619 603 -475 53 C ATOM 919 CD1 ILE A 119 -29.332 26.632 -12.748 1.00 58.05 C ANISOU 919 CD1 ILE A 119 7453 9824 4779 660 -266 88 C ATOM 920 N ALA A 120 -34.768 28.475 -13.485 1.00 53.50 N ANISOU 920 N ALA A 120 6757 9349 4219 469 -671 284 N ATOM 921 CA ALA A 120 -36.180 28.303 -13.826 1.00 58.02 C ANISOU 921 CA ALA A 120 7289 10022 4732 440 -807 221 C ATOM 922 C ALA A 120 -36.745 29.510 -14.596 1.00 61.63 C ANISOU 922 C ALA A 120 7689 10621 5105 522 -852 401 C ATOM 923 O ALA A 120 -37.396 29.306 -15.619 1.00 66.46 O ANISOU 923 O ALA A 120 8286 11423 5543 558 -955 369 O ATOM 924 CB ALA A 120 -36.984 28.002 -12.552 1.00 57.53 C ANISOU 924 CB ALA A 120 7182 9818 4860 337 -851 140 C ATOM 925 N LEU A 121 -36.422 30.733 -14.134 1.00 60.86 N ANISOU 925 N LEU A 121 7572 10433 5120 558 -775 588 N ATOM 926 CA LEU A 121 -36.726 32.003 -14.806 1.00 64.68 C ANISOU 926 CA LEU A 121 8038 11014 5525 658 -799 782 C ATOM 927 C LEU A 121 -36.061 32.119 -16.189 1.00 67.35 C ANISOU 927 C LEU A 121 8448 11525 5617 740 -772 850 C ATOM 928 O LEU A 121 -36.720 32.558 -17.129 1.00 69.19 O ANISOU 928 O LEU A 121 8676 11931 5683 831 -862 919 O ATOM 929 CB LEU A 121 -36.280 33.185 -13.913 1.00 67.14 C ANISOU 929 CB LEU A 121 8351 11151 6008 665 -695 957 C ATOM 930 CG LEU A 121 -37.113 33.384 -12.629 1.00 69.43 C ANISOU 930 CG LEU A 121 8570 11300 6512 624 -728 942 C ATOM 931 CD1 LEU A 121 -36.350 34.227 -11.584 1.00 69.29 C ANISOU 931 CD1 LEU A 121 8583 11095 6648 616 -605 1089 C ATOM 932 CD2 LEU A 121 -38.521 33.945 -12.928 1.00 72.95 C ANISOU 932 CD2 LEU A 121 8935 11873 6910 703 -861 970 C ATOM 933 N ASP A 122 -34.783 31.707 -16.281 1.00 68.79 N ANISOU 933 N ASP A 122 8692 11682 5763 719 -648 831 N ATOM 934 CA ASP A 122 -33.950 31.746 -17.485 1.00 70.26 C ANISOU 934 CA ASP A 122 8949 12037 5710 792 -595 897 C ATOM 935 C ASP A 122 -34.533 30.886 -18.627 1.00 68.90 C ANISOU 935 C ASP A 122 8796 12060 5323 819 -719 733 C ATOM 936 O ASP A 122 -34.661 31.377 -19.748 1.00 70.85 O ANISOU 936 O ASP A 122 9080 12497 5344 908 -760 812 O ATOM 937 CB ASP A 122 -32.496 31.327 -17.149 1.00 72.25 C ANISOU 937 CB ASP A 122 9232 12237 5984 758 -428 888 C ATOM 938 CG ASP A 122 -31.490 31.576 -18.270 1.00 78.86 C ANISOU 938 CG ASP A 122 10136 13244 6582 824 -336 983 C ATOM 939 OD1 ASP A 122 -31.516 32.697 -18.821 1.00 79.86 O ANISOU 939 OD1 ASP A 122 10297 13373 6673 853 -259 1200 O ATOM 940 OD2 ASP A 122 -30.663 30.672 -18.520 1.00 80.27 O1- ANISOU 940 OD2 ASP A 122 10349 13546 6604 848 -329 840 O1- ATOM 941 N ARG A 123 -34.906 29.636 -18.300 1.00 64.55 N ANISOU 941 N ARG A 123 8234 11462 4830 742 -776 503 N ATOM 942 CA ARG A 123 -35.537 28.679 -19.212 1.00 63.27 C ANISOU 942 CA ARG A 123 8097 11466 4478 737 -897 317 C ATOM 943 C ARG A 123 -36.969 29.078 -19.614 1.00 67.67 C ANISOU 943 C ARG A 123 8572 12170 4970 759 -1066 345 C ATOM 944 O ARG A 123 -37.355 28.819 -20.753 1.00 72.14 O ANISOU 944 O ARG A 123 9153 12961 5297 808 -1165 295 O ATOM 945 CB ARG A 123 -35.546 27.282 -18.562 1.00 58.53 C ANISOU 945 CB ARG A 123 7525 10734 3980 631 -908 71 C ATOM 946 CG ARG A 123 -34.157 26.647 -18.375 1.00 56.60 C ANISOU 946 CG ARG A 123 7367 10398 3742 651 -765 6 C ATOM 947 CD ARG A 123 -34.249 25.378 -17.519 1.00 56.49 C ANISOU 947 CD ARG A 123 7398 10199 3866 567 -771 -197 C ATOM 948 NE ARG A 123 -32.992 24.622 -17.488 1.00 59.52 N ANISOU 948 NE ARG A 123 7881 10538 4195 623 -662 -302 N ATOM 949 CZ ARG A 123 -32.804 23.480 -16.805 1.00 62.54 C ANISOU 949 CZ ARG A 123 8341 10740 4680 594 -635 -458 C ATOM 950 NH1 ARG A 123 -33.775 22.947 -16.048 1.00 61.07 N1+ ANISOU 950 NH1 ARG A 123 8151 10397 4656 484 -700 -522 N1+ ATOM 951 NH2 ARG A 123 -31.625 22.855 -16.887 1.00 65.13 N1+ ANISOU 951 NH2 ARG A 123 8755 11047 4943 685 -536 -543 N1+ ATOM 952 N CYS A 124 -37.724 29.699 -18.690 1.00 67.84 N ANISOU 952 N CYS A 124 8498 12083 5193 733 -1103 418 N ATOM 953 CA CYS A 124 -39.088 30.181 -18.920 1.00 68.16 C ANISOU 953 CA CYS A 124 8431 12280 5188 775 -1262 445 C ATOM 954 C CYS A 124 -39.126 31.350 -19.922 1.00 71.56 C ANISOU 954 C CYS A 124 8887 12880 5422 946 -1282 668 C ATOM 955 O CYS A 124 -39.974 31.347 -20.812 1.00 74.59 O ANISOU 955 O CYS A 124 9210 13497 5634 1019 -1436 655 O ATOM 956 CB CYS A 124 -39.794 30.505 -17.588 1.00 65.43 C ANISOU 956 CB CYS A 124 7982 11774 5107 728 -1269 484 C ATOM 957 SG CYS A 124 -41.538 30.965 -17.788 1.00 70.56 S ANISOU 957 SG CYS A 124 8456 12625 5728 795 -1457 508 S ATOM 958 N ILE A 125 -38.161 32.278 -19.806 1.00 69.68 N ANISOU 958 N ILE A 125 8740 12534 5199 1009 -1127 873 N ATOM 959 CA ILE A 125 -37.947 33.393 -20.731 1.00 72.80 C ANISOU 959 CA ILE A 125 9198 13052 5410 1169 -1117 1111 C ATOM 960 C ILE A 125 -37.603 32.941 -22.168 1.00 76.54 C ANISOU 960 C ILE A 125 9756 13759 5566 1222 -1139 1066 C ATOM 961 O ILE A 125 -38.060 33.583 -23.110 1.00 79.92 O ANISOU 961 O ILE A 125 10206 14396 5765 1360 -1231 1177 O ATOM 962 CB ILE A 125 -36.858 34.365 -20.179 1.00 74.03 C ANISOU 962 CB ILE A 125 9437 12995 5697 1181 -925 1337 C ATOM 963 CG1 ILE A 125 -37.421 35.165 -18.979 1.00 73.38 C ANISOU 963 CG1 ILE A 125 9281 12703 5898 1154 -921 1388 C ATOM 964 CG2 ILE A 125 -36.225 35.336 -21.202 1.00 77.84 C ANISOU 964 CG2 ILE A 125 10033 13576 5966 1332 -878 1590 C ATOM 965 CD1 ILE A 125 -36.342 35.783 -18.076 1.00 71.86 C ANISOU 965 CD1 ILE A 125 9167 12276 5861 1122 -732 1561 C ATOM 966 N CYS A 126 -36.856 31.832 -22.314 1.00 75.74 N ANISOU 966 N CYS A 126 9708 13636 5435 1130 -1058 899 N ATOM 967 CA CYS A 126 -36.522 31.232 -23.610 1.00 77.28 C ANISOU 967 CA CYS A 126 9990 14049 5323 1179 -1064 832 C ATOM 968 C CYS A 126 -37.747 30.616 -24.309 1.00 80.87 C ANISOU 968 C CYS A 126 10389 14745 5591 1196 -1284 664 C ATOM 969 O CYS A 126 -37.910 30.814 -25.511 1.00 87.79 O ANISOU 969 O CYS A 126 11316 15866 6173 1307 -1351 718 O ATOM 970 CB CYS A 126 -35.433 30.149 -23.486 1.00 76.44 C ANISOU 970 CB CYS A 126 9942 13857 5245 1091 -934 659 C ATOM 971 SG CYS A 126 -33.848 30.892 -23.033 1.00 80.60 S ANISOU 971 SG CYS A 126 10517 14203 5904 1080 -672 841 S ATOM 972 N VAL A 127 -38.560 29.861 -23.551 1.00 77.71 N ANISOU 972 N VAL A 127 9884 14290 5350 1076 -1395 456 N ATOM 973 CA VAL A 127 -39.663 29.057 -24.077 1.00 79.41 C ANISOU 973 CA VAL A 127 10028 14741 5404 1045 -1600 255 C ATOM 974 C VAL A 127 -40.927 29.884 -24.380 1.00 82.28 C ANISOU 974 C VAL A 127 10273 15294 5695 1172 -1759 404 C ATOM 975 O VAL A 127 -41.531 29.675 -25.432 1.00 88.10 O ANISOU 975 O VAL A 127 10988 16215 6271 1213 -1882 342 O ATOM 976 CB VAL A 127 -39.998 27.890 -23.102 1.00 79.01 C ANISOU 976 CB VAL A 127 9916 14553 5553 848 -1642 -20 C ATOM 977 CG1 VAL A 127 -41.320 27.143 -23.376 1.00 69.78 C ANISOU 977 CG1 VAL A 127 8674 13628 4212 773 -1841 -261 C ATOM 978 CG2 VAL A 127 -38.846 26.872 -23.074 1.00 79.06 C ANISOU 978 CG2 VAL A 127 10055 14352 5633 768 -1478 -141 C ATOM 979 N LEU A 128 -41.293 30.807 -23.474 1.00 77.55 N ANISOU 979 N LEU A 128 9608 14539 5320 1219 -1721 590 N ATOM 980 CA LEU A 128 -42.467 31.671 -23.617 1.00 78.65 C ANISOU 980 CA LEU A 128 9623 14840 5422 1360 -1871 721 C ATOM 981 C LEU A 128 -42.187 32.887 -24.518 1.00 81.09 C ANISOU 981 C LEU A 128 10051 15166 5593 1559 -1812 996 C ATOM 982 O LEU A 128 -43.119 33.347 -25.179 1.00 81.30 O ANISOU 982 O LEU A 128 10025 15343 5523 1680 -1936 1043 O ATOM 983 CB LEU A 128 -42.977 32.136 -22.230 1.00 75.88 C ANISOU 983 CB LEU A 128 9161 14276 5395 1326 -1840 781 C ATOM 984 CG LEU A 128 -43.855 31.117 -21.461 1.00 73.51 C ANISOU 984 CG LEU A 128 8680 13989 5260 1160 -1951 532 C ATOM 985 CD1 LEU A 128 -43.120 29.828 -21.031 1.00 66.73 C ANISOU 985 CD1 LEU A 128 7881 13028 4445 937 -1901 261 C ATOM 986 CD2 LEU A 128 -44.562 31.799 -20.270 1.00 73.73 C ANISOU 986 CD2 LEU A 128 8622 13800 5592 1154 -1888 629 C ATOM 987 N HIS A 129 -40.936 33.385 -24.526 1.00 81.57 N ANISOU 987 N HIS A 129 10272 15080 5642 1591 -1619 1180 N ATOM 988 CA HIS A 129 -40.535 34.619 -25.211 1.00 82.49 C ANISOU 988 CA HIS A 129 10533 15177 5634 1752 -1527 1453 C ATOM 989 C HIS A 129 -39.237 34.426 -26.032 1.00 83.11 C ANISOU 989 C HIS A 129 10771 15252 5555 1705 -1368 1451 C ATOM 990 O HIS A 129 -38.261 35.130 -25.768 1.00 81.55 O ANISOU 990 O HIS A 129 10676 14903 5408 1687 -1172 1608 O ATOM 991 CB HIS A 129 -40.422 35.775 -24.179 1.00 81.28 C ANISOU 991 CB HIS A 129 10419 14817 5646 1837 -1418 1725 C ATOM 992 CG HIS A 129 -41.574 35.915 -23.213 1.00 80.28 C ANISOU 992 CG HIS A 129 10124 14661 5718 1856 -1537 1696 C ATOM 993 CD2 HIS A 129 -41.642 35.735 -21.849 1.00 79.57 C ANISOU 993 CD2 HIS A 129 9979 14314 5940 1754 -1455 1680 C ATOM 994 ND1 HIS A 129 -42.856 36.256 -23.608 1.00 83.84 N ANISOU 994 ND1 HIS A 129 10433 15275 6147 1948 -1728 1634 N ATOM 995 CE1 HIS A 129 -43.618 36.260 -22.511 1.00 81.79 C ANISOU 995 CE1 HIS A 129 10027 14959 6090 1943 -1783 1614 C ATOM 996 NE2 HIS A 129 -42.949 35.951 -21.406 1.00 79.97 N ANISOU 996 NE2 HIS A 129 9858 14440 6087 1815 -1609 1634 N ATOM 997 N PRO A 130 -39.215 33.487 -27.012 1.00 85.88 N ANISOU 997 N PRO A 130 11142 15776 5713 1679 -1440 1269 N ATOM 998 CA PRO A 130 -38.018 33.239 -27.845 1.00 87.19 C ANISOU 998 CA PRO A 130 11453 15953 5721 1648 -1280 1257 C ATOM 999 C PRO A 130 -37.591 34.430 -28.728 1.00 89.35 C ANISOU 999 C PRO A 130 11880 16210 5859 1772 -1150 1542 C ATOM 1000 O PRO A 130 -36.395 34.603 -28.958 1.00 88.88 O ANISOU 1000 O PRO A 130 11929 16085 5755 1734 -947 1619 O ATOM 1001 CB PRO A 130 -38.405 32.016 -28.694 1.00 88.74 C ANISOU 1001 CB PRO A 130 11629 16339 5748 1598 -1417 978 C ATOM 1002 CG PRO A 130 -39.920 32.091 -28.802 1.00 91.10 C ANISOU 1002 CG PRO A 130 11805 16769 6038 1662 -1638 957 C ATOM 1003 CD PRO A 130 -40.331 32.641 -27.442 1.00 89.62 C ANISOU 1003 CD PRO A 130 11502 16449 6101 1670 -1661 1060 C ATOM 1004 N VAL A 131 -38.572 35.241 -29.162 1.00 91.60 N ANISOU 1004 N VAL A 131 12175 16555 6075 1918 -1255 1698 N ATOM 1005 CA VAL A 131 -38.380 36.470 -29.935 1.00 94.58 C ANISOU 1005 CA VAL A 131 12724 16889 6321 2037 -1127 1983 C ATOM 1006 C VAL A 131 -37.715 37.595 -29.110 1.00 95.29 C ANISOU 1006 C VAL A 131 12888 16729 6589 2018 -928 2218 C ATOM 1007 O VAL A 131 -36.969 38.389 -29.682 1.00 96.24 O ANISOU 1007 O VAL A 131 13163 16768 6637 2004 -722 2389 O ATOM 1008 CB VAL A 131 -39.734 36.975 -30.517 1.00 93.59 C ANISOU 1008 CB VAL A 131 12594 16883 6082 2218 -1298 2089 C ATOM 1009 CG1 VAL A 131 -39.675 38.349 -31.222 1.00 92.83 C ANISOU 1009 CG1 VAL A 131 12705 16708 5858 2346 -1158 2402 C ATOM 1010 CG2 VAL A 131 -40.335 35.939 -31.486 1.00 92.83 C ANISOU 1010 CG2 VAL A 131 12430 17051 5788 2215 -1483 1852 C ATOM 1011 N TRP A 132 -37.949 37.616 -27.785 1.00 96.91 N ANISOU 1011 N TRP A 132 12982 16810 7028 2004 -978 2224 N ATOM 1012 CA TRP A 132 -37.253 38.505 -26.856 1.00 94.49 C ANISOU 1012 CA TRP A 132 12743 16258 6902 1966 -791 2424 C ATOM 1013 C TRP A 132 -35.829 38.000 -26.568 1.00 93.72 C ANISOU 1013 C TRP A 132 12653 16105 6850 1793 -606 2342 C ATOM 1014 O TRP A 132 -34.898 38.800 -26.596 1.00 93.99 O ANISOU 1014 O TRP A 132 12788 15982 6941 1741 -392 2526 O ATOM 1015 CB TRP A 132 -38.075 38.660 -25.559 1.00 91.08 C ANISOU 1015 CB TRP A 132 12183 15721 6703 1993 -896 2426 C ATOM 1016 CG TRP A 132 -37.557 39.659 -24.563 1.00 90.01 C ANISOU 1016 CG TRP A 132 12124 15321 6754 1960 -714 2633 C ATOM 1017 CD1 TRP A 132 -37.899 40.967 -24.531 1.00 91.07 C ANISOU 1017 CD1 TRP A 132 12384 15276 6943 2079 -643 2896 C ATOM 1018 CD2 TRP A 132 -36.543 39.488 -23.521 1.00 88.06 C ANISOU 1018 CD2 TRP A 132 11833 14874 6751 1755 -566 2534 C ATOM 1019 CE2 TRP A 132 -36.338 40.749 -22.880 1.00 86.96 C ANISOU 1019 CE2 TRP A 132 11789 14454 6797 1744 -414 2743 C ATOM 1020 CE3 TRP A 132 -35.762 38.403 -23.057 1.00 87.76 C ANISOU 1020 CE3 TRP A 132 11690 14841 6814 1577 -545 2274 C ATOM 1021 NE1 TRP A 132 -37.194 41.609 -23.535 1.00 88.75 N ANISOU 1021 NE1 TRP A 132 12136 14712 6873 1960 -461 2985 N ATOM 1022 CZ2 TRP A 132 -35.412 40.923 -21.836 1.00 88.17 C ANISOU 1022 CZ2 TRP A 132 11916 14362 7223 1548 -256 2687 C ATOM 1023 CZ3 TRP A 132 -34.817 38.569 -22.022 1.00 87.49 C ANISOU 1023 CZ3 TRP A 132 11630 14565 7047 1411 -391 2236 C ATOM 1024 CH2 TRP A 132 -34.644 39.825 -21.410 1.00 87.86 C ANISOU 1024 CH2 TRP A 132 11753 14364 7267 1391 -254 2436 C ATOM 1025 N ALA A 133 -35.692 36.689 -26.297 1.00 93.73 N ANISOU 1025 N ALA A 133 12552 16233 6829 1701 -679 2063 N ATOM 1026 CA ALA A 133 -34.446 36.037 -25.894 1.00 95.62 C ANISOU 1026 CA ALA A 133 12782 16427 7123 1560 -515 1961 C ATOM 1027 C ALA A 133 -33.317 36.113 -26.938 1.00101.13 C ANISOU 1027 C ALA A 133 13612 17169 7643 1551 -312 2064 C ATOM 1028 O ALA A 133 -32.167 36.315 -26.555 1.00101.03 O ANISOU 1028 O ALA A 133 13626 17046 7713 1461 -98 2158 O ATOM 1029 CB ALA A 133 -34.744 34.581 -25.504 1.00 97.00 C ANISOU 1029 CB ALA A 133 12847 16686 7323 1478 -639 1623 C ATOM 1030 N GLN A 134 -33.656 36.004 -28.233 1.00103.79 N ANISOU 1030 N GLN A 134 14022 17661 7752 1628 -371 2035 N ATOM 1031 CA GLN A 134 -32.694 36.093 -29.339 1.00106.79 C ANISOU 1031 CA GLN A 134 14527 18097 7951 1616 -178 2115 C ATOM 1032 C GLN A 134 -32.090 37.502 -29.547 1.00108.45 C ANISOU 1032 C GLN A 134 14876 18165 8163 1638 -3 2442 C ATOM 1033 O GLN A 134 -31.081 37.603 -30.244 1.00111.05 O ANISOU 1033 O GLN A 134 15298 18500 8398 1580 212 2532 O ATOM 1034 CB GLN A 134 -33.352 35.539 -30.622 1.00110.76 C ANISOU 1034 CB GLN A 134 15081 18805 8197 1695 -297 1997 C ATOM 1035 CG GLN A 134 -34.478 36.423 -31.197 1.00116.56 C ANISOU 1035 CG GLN A 134 15860 19587 8840 1837 -471 2123 C ATOM 1036 CD GLN A 134 -35.235 35.797 -32.369 1.00119.94 C ANISOU 1036 CD GLN A 134 16269 20240 9064 1890 -662 1920 C ATOM 1037 NE2 GLN A 134 -36.035 36.613 -33.057 1.00122.06 N ANISOU 1037 NE2 GLN A 134 16618 20602 9157 2023 -752 2055 N ATOM 1038 OE1 GLN A 134 -35.124 34.605 -32.647 1.00119.97 O ANISOU 1038 OE1 GLN A 134 16194 20327 9062 1811 -726 1643 O ATOM 1039 N ASN A 135 -32.701 38.545 -28.954 1.00109.23 N ANISOU 1039 N ASN A 135 14999 18130 8373 1715 -80 2616 N ATOM 1040 CA ASN A 135 -32.277 39.946 -29.066 1.00113.19 C ANISOU 1040 CA ASN A 135 15669 18458 8882 1741 81 2926 C ATOM 1041 C ASN A 135 -31.750 40.523 -27.739 1.00111.60 C ANISOU 1041 C ASN A 135 15453 18014 8936 1638 223 3048 C ATOM 1042 O ASN A 135 -30.971 41.473 -27.806 1.00115.19 O ANISOU 1042 O ASN A 135 16061 18293 9415 1606 411 3288 O ATOM 1043 CB ASN A 135 -33.465 40.801 -29.570 1.00118.38 C ANISOU 1043 CB ASN A 135 16405 19118 9456 1933 -87 3063 C ATOM 1044 CG ASN A 135 -33.854 40.516 -31.024 1.00121.90 C ANISOU 1044 CG ASN A 135 16946 19762 9609 2026 -139 3058 C ATOM 1045 ND2 ASN A 135 -33.081 41.044 -31.975 1.00124.07 N ANISOU 1045 ND2 ASN A 135 17422 19965 9752 2039 39 3289 N ATOM 1046 OD1 ASN A 135 -34.846 39.843 -31.289 1.00122.17 O ANISOU 1046 OD1 ASN A 135 16880 20006 9532 2072 -331 2845 O ATOM 1047 N HIS A 136 -32.183 39.992 -26.578 1.00105.75 N ANISOU 1047 N HIS A 136 14546 17252 8383 1576 145 2889 N ATOM 1048 CA HIS A 136 -31.946 40.614 -25.267 1.00103.92 C ANISOU 1048 CA HIS A 136 14287 16753 8442 1459 261 2965 C ATOM 1049 C HIS A 136 -31.207 39.713 -24.266 1.00 96.77 C ANISOU 1049 C HIS A 136 13200 15781 7786 1277 282 2699 C ATOM 1050 O HIS A 136 -30.451 40.257 -23.460 1.00 94.33 O ANISOU 1050 O HIS A 136 12869 15257 7715 1128 431 2729 O ATOM 1051 CB HIS A 136 -33.278 41.088 -24.653 1.00108.10 C ANISOU 1051 CB HIS A 136 14816 17142 9116 1581 109 3052 C ATOM 1052 CG HIS A 136 -34.048 42.097 -25.469 1.00117.02 C ANISOU 1052 CG HIS A 136 16125 18264 10075 1771 84 3301 C ATOM 1053 CD2 HIS A 136 -34.057 43.475 -25.455 1.00120.39 C ANISOU 1053 CD2 HIS A 136 16741 18454 10546 1804 227 3567 C ATOM 1054 ND1 HIS A 136 -34.983 41.732 -26.421 1.00120.58 N ANISOU 1054 ND1 HIS A 136 16568 18910 10337 1925 -108 3239 N ATOM 1055 CE1 HIS A 136 -35.489 42.854 -26.934 1.00123.47 C ANISOU 1055 CE1 HIS A 136 17103 19181 10628 2065 -90 3465 C ATOM 1056 NE2 HIS A 136 -34.974 43.952 -26.395 1.00123.29 N ANISOU 1056 NE2 HIS A 136 17215 18885 10747 1997 115 3667 N ATOM 1057 N ARG A 137 -31.415 38.383 -24.312 1.00 90.15 N ANISOU 1057 N ARG A 137 12241 15112 6899 1283 142 2439 N ATOM 1058 CA ARG A 137 -30.755 37.423 -23.418 1.00 82.37 C ANISOU 1058 CA ARG A 137 11108 14060 6129 1140 160 2194 C ATOM 1059 C ARG A 137 -29.319 37.152 -23.901 1.00 82.37 C ANISOU 1059 C ARG A 137 11116 14136 6046 1049 373 2173 C ATOM 1060 O ARG A 137 -29.087 36.217 -24.668 1.00 83.84 O ANISOU 1060 O ARG A 137 11306 14533 6018 1092 368 2053 O ATOM 1061 CB ARG A 137 -31.618 36.147 -23.280 1.00 77.29 C ANISOU 1061 CB ARG A 137 10367 13542 5459 1182 -56 1933 C ATOM 1062 CG ARG A 137 -31.046 35.070 -22.342 1.00 74.05 C ANISOU 1062 CG ARG A 137 9839 13064 5230 1065 -41 1681 C ATOM 1063 CD ARG A 137 -31.982 33.862 -22.229 1.00 73.29 C ANISOU 1063 CD ARG A 137 9696 13091 5061 1101 -235 1434 C ATOM 1064 NE ARG A 137 -31.343 32.729 -21.552 1.00 72.00 N ANISOU 1064 NE ARG A 137 9456 12839 5063 1012 -224 1202 N ATOM 1065 CZ ARG A 137 -30.598 31.765 -22.118 1.00 75.27 C ANISOU 1065 CZ ARG A 137 9882 13342 5376 1007 -143 1056 C ATOM 1066 NH1 ARG A 137 -30.332 31.771 -23.432 1.00 79.79 N1+ ANISOU 1066 NH1 ARG A 137 10531 14104 5682 1071 -58 1111 N1+ ATOM 1067 NH2 ARG A 137 -30.117 30.779 -21.350 1.00 73.33 N1+ ANISOU 1067 NH2 ARG A 137 9581 12993 5287 954 -140 860 N1+ ATOM 1068 N THR A 138 -28.397 38.011 -23.446 1.00 81.61 N ANISOU 1068 N THR A 138 11013 13876 6121 915 565 2277 N ATOM 1069 CA THR A 138 -26.977 38.002 -23.784 1.00 81.84 C ANISOU 1069 CA THR A 138 11024 13984 6088 812 792 2281 C ATOM 1070 C THR A 138 -26.142 37.708 -22.524 1.00 78.39 C ANISOU 1070 C THR A 138 10417 13457 5913 676 845 2101 C ATOM 1071 O THR A 138 -26.633 37.860 -21.404 1.00 74.38 O ANISOU 1071 O THR A 138 9835 12784 5643 644 734 2017 O ATOM 1072 CB THR A 138 -26.541 39.393 -24.334 1.00 85.79 C ANISOU 1072 CB THR A 138 11662 14400 6533 747 1003 2568 C ATOM 1073 CG2 THR A 138 -27.329 39.827 -25.580 1.00 88.51 C ANISOU 1073 CG2 THR A 138 12198 14833 6601 915 945 2770 C ATOM 1074 OG1 THR A 138 -26.625 40.422 -23.360 1.00 84.75 O ANISOU 1074 OG1 THR A 138 11527 13993 6681 643 1035 2653 O ATOM 1075 N VAL A 139 -24.876 37.311 -22.740 1.00 79.83 N ANISOU 1075 N VAL A 139 10530 13767 6034 606 1021 2044 N ATOM 1076 CA VAL A 139 -23.866 37.102 -21.696 1.00 76.76 C ANISOU 1076 CA VAL A 139 9967 13329 5868 491 1087 1891 C ATOM 1077 C VAL A 139 -23.577 38.380 -20.876 1.00 74.09 C ANISOU 1077 C VAL A 139 9611 12778 5761 325 1192 2024 C ATOM 1078 O VAL A 139 -23.387 38.281 -19.664 1.00 69.73 O ANISOU 1078 O VAL A 139 8946 12099 5451 255 1138 1913 O ATOM 1079 CB VAL A 139 -22.545 36.551 -22.315 1.00 77.62 C ANISOU 1079 CB VAL A 139 9992 13665 5836 480 1254 1799 C ATOM 1080 CG1 VAL A 139 -21.294 36.623 -21.412 1.00 77.03 C ANISOU 1080 CG1 VAL A 139 9729 13562 5977 341 1375 1714 C ATOM 1081 CG2 VAL A 139 -22.744 35.106 -22.809 1.00 75.81 C ANISOU 1081 CG2 VAL A 139 9755 13593 5456 638 1125 1583 C ATOM 1082 N SER A 140 -23.604 39.548 -21.543 1.00 77.82 N ANISOU 1082 N SER A 140 10213 13201 6153 258 1347 2262 N ATOM 1083 CA SER A 140 -23.441 40.870 -20.936 1.00 79.70 C ANISOU 1083 CA SER A 140 10469 13211 6601 84 1462 2388 C ATOM 1084 C SER A 140 -24.563 41.241 -19.948 1.00 79.67 C ANISOU 1084 C SER A 140 10496 12975 6798 127 1280 2381 C ATOM 1085 O SER A 140 -24.275 41.900 -18.950 1.00 79.62 O ANISOU 1085 O SER A 140 10409 12808 7034 -3 1296 2326 O ATOM 1086 CB SER A 140 -23.329 41.927 -22.052 1.00 83.65 C ANISOU 1086 CB SER A 140 11160 13668 6954 26 1657 2663 C ATOM 1087 OG SER A 140 -22.060 41.854 -22.668 1.00 88.06 O ANISOU 1087 OG SER A 140 11698 14464 7298 -4 1832 2676 O ATOM 1088 N LEU A 141 -25.802 40.792 -20.222 1.00 77.44 N ANISOU 1088 N LEU A 141 10319 12696 6411 308 1104 2425 N ATOM 1089 CA LEU A 141 -26.944 40.927 -19.317 1.00 74.90 C ANISOU 1089 CA LEU A 141 10005 12186 6269 362 933 2405 C ATOM 1090 C LEU A 141 -26.864 39.916 -18.161 1.00 77.02 C ANISOU 1090 C LEU A 141 10098 12461 6704 348 798 2147 C ATOM 1091 O LEU A 141 -27.020 40.317 -17.009 1.00 77.75 O ANISOU 1091 O LEU A 141 10149 12372 7022 294 743 2104 O ATOM 1092 CB LEU A 141 -28.264 40.784 -20.117 1.00 72.22 C ANISOU 1092 CB LEU A 141 9786 11898 5758 566 775 2504 C ATOM 1093 CG LEU A 141 -29.565 40.949 -19.290 1.00 68.04 C ANISOU 1093 CG LEU A 141 9269 11196 5388 646 613 2520 C ATOM 1094 CD1 LEU A 141 -29.698 42.355 -18.669 1.00 69.76 C ANISOU 1094 CD1 LEU A 141 9610 11149 5748 578 743 2717 C ATOM 1095 CD2 LEU A 141 -30.808 40.566 -20.114 1.00 65.56 C ANISOU 1095 CD2 LEU A 141 9008 11022 4881 857 427 2558 C ATOM 1096 N ALA A 142 -26.634 38.635 -18.502 1.00 78.47 N ANISOU 1096 N ALA A 142 10198 12846 6772 402 751 1976 N ATOM 1097 CA ALA A 142 -26.646 37.486 -17.594 1.00 75.60 C ANISOU 1097 CA ALA A 142 9701 12474 6549 403 635 1741 C ATOM 1098 C ALA A 142 -25.654 37.581 -16.427 1.00 78.36 C ANISOU 1098 C ALA A 142 9929 12741 7102 254 742 1678 C ATOM 1099 O ALA A 142 -26.037 37.272 -15.301 1.00 77.57 O ANISOU 1099 O ALA A 142 9757 12528 7188 231 649 1559 O ATOM 1100 CB ALA A 142 -26.401 36.206 -18.400 1.00 73.98 C ANISOU 1100 CB ALA A 142 9466 12482 6162 500 585 1576 C ATOM 1101 N MET A 143 -24.424 38.040 -16.713 1.00 81.32 N ANISOU 1101 N MET A 143 10274 13187 7435 146 940 1751 N ATOM 1102 CA MET A 143 -23.352 38.238 -15.733 1.00 82.40 C ANISOU 1102 CA MET A 143 10274 13274 7758 -13 1041 1691 C ATOM 1103 C MET A 143 -23.614 39.365 -14.713 1.00 80.46 C ANISOU 1103 C MET A 143 10075 12774 7724 -114 1020 1766 C ATOM 1104 O MET A 143 -22.955 39.371 -13.675 1.00 77.41 O ANISOU 1104 O MET A 143 9580 12311 7521 -186 982 1647 O ATOM 1105 CB MET A 143 -22.021 38.470 -16.479 1.00 89.55 C ANISOU 1105 CB MET A 143 11136 14316 8571 -137 1272 1771 C ATOM 1106 CG MET A 143 -21.465 37.211 -17.171 1.00 95.24 C ANISOU 1106 CG MET A 143 11781 15309 9097 -43 1322 1670 C ATOM 1107 SD MET A 143 -20.943 35.863 -16.070 1.00 97.96 S ANISOU 1107 SD MET A 143 11904 15769 9548 12 1248 1395 S ATOM 1108 CE MET A 143 -19.514 36.619 -15.252 1.00 98.69 C ANISOU 1108 CE MET A 143 11831 15803 9862 -224 1376 1401 C ATOM 1109 N LYS A 144 -24.562 40.273 -15.003 1.00 83.44 N ANISOU 1109 N LYS A 144 10621 13015 8065 -103 1043 1961 N ATOM 1110 CA LYS A 144 -24.966 41.357 -14.106 1.00 82.39 C ANISOU 1110 CA LYS A 144 10559 12624 8123 -190 1051 2042 C ATOM 1111 C LYS A 144 -26.095 40.925 -13.156 1.00 79.32 C ANISOU 1111 C LYS A 144 10144 12130 7865 -93 850 1930 C ATOM 1112 O LYS A 144 -26.027 41.248 -11.971 1.00 79.47 O ANISOU 1112 O LYS A 144 10089 12030 8074 -184 829 1834 O ATOM 1113 CB LYS A 144 -25.400 42.586 -14.931 1.00 84.69 C ANISOU 1113 CB LYS A 144 11062 12793 8322 -164 1135 2292 C ATOM 1114 CG LYS A 144 -24.263 43.208 -15.757 1.00 89.09 C ANISOU 1114 CG LYS A 144 11680 13394 8775 -304 1373 2433 C ATOM 1115 CD LYS A 144 -24.756 44.340 -16.668 1.00 93.68 C ANISOU 1115 CD LYS A 144 12514 13813 9267 -254 1451 2699 C ATOM 1116 CE LYS A 144 -23.624 44.971 -17.489 1.00 98.52 C ANISOU 1116 CE LYS A 144 13216 14408 9809 -440 1720 2853 C ATOM 1117 NZ LYS A 144 -24.137 46.009 -18.398 1.00101.82 N1+ ANISOU 1117 NZ LYS A 144 13920 14620 10147 -385 1807 3129 N1+ ATOM 1118 N VAL A 145 -27.112 40.223 -13.685 1.00 76.95 N ANISOU 1118 N VAL A 145 9898 11884 7456 82 702 1936 N ATOM 1119 CA VAL A 145 -28.321 39.851 -12.941 1.00 76.31 C ANISOU 1119 CA VAL A 145 9806 11696 7494 162 531 1862 C ATOM 1120 C VAL A 145 -28.181 38.558 -12.105 1.00 76.40 C ANISOU 1120 C VAL A 145 9678 11751 7598 147 437 1636 C ATOM 1121 O VAL A 145 -28.935 38.401 -11.144 1.00 77.33 O ANISOU 1121 O VAL A 145 9774 11750 7857 156 337 1564 O ATOM 1122 CB VAL A 145 -29.555 39.719 -13.877 1.00 77.59 C ANISOU 1122 CB VAL A 145 10045 11934 7504 340 401 1927 C ATOM 1123 CG1 VAL A 145 -29.940 41.072 -14.497 1.00 80.07 C ANISOU 1123 CG1 VAL A 145 10519 12182 7724 388 486 2172 C ATOM 1124 CG2 VAL A 145 -29.410 38.649 -14.971 1.00 78.92 C ANISOU 1124 CG2 VAL A 145 10170 12340 7477 413 343 1820 C ATOM 1125 N ILE A 146 -27.206 37.689 -12.434 1.00 76.19 N ANISOU 1125 N ILE A 146 9567 11891 7490 136 473 1525 N ATOM 1126 CA ILE A 146 -26.883 36.476 -11.666 1.00 72.51 C ANISOU 1126 CA ILE A 146 8998 11453 7101 149 389 1323 C ATOM 1127 C ILE A 146 -26.159 36.774 -10.329 1.00 68.06 C ANISOU 1127 C ILE A 146 8346 10791 6721 25 442 1269 C ATOM 1128 O ILE A 146 -26.092 35.893 -9.472 1.00 64.75 O ANISOU 1128 O ILE A 146 7859 10363 6380 44 364 1121 O ATOM 1129 CB ILE A 146 -26.032 35.485 -12.517 1.00 74.66 C ANISOU 1129 CB ILE A 146 9221 11933 7215 216 407 1216 C ATOM 1130 CG1 ILE A 146 -26.075 34.040 -11.971 1.00 72.94 C ANISOU 1130 CG1 ILE A 146 8974 11714 7024 297 274 1026 C ATOM 1131 CG2 ILE A 146 -24.573 35.938 -12.747 1.00 76.44 C ANISOU 1131 CG2 ILE A 146 9343 12257 7446 125 564 1209 C ATOM 1132 CD1 ILE A 146 -25.736 32.977 -13.023 1.00 74.05 C ANISOU 1132 CD1 ILE A 146 9096 12029 7010 388 289 906 C ATOM 1133 N VAL A 147 -25.683 38.021 -10.155 1.00 66.23 N ANISOU 1133 N VAL A 147 8128 10484 6554 -106 572 1383 N ATOM 1134 CA VAL A 147 -25.116 38.558 -8.916 1.00 65.49 C ANISOU 1134 CA VAL A 147 7951 10299 6631 -243 612 1320 C ATOM 1135 C VAL A 147 -26.183 38.784 -7.819 1.00 65.11 C ANISOU 1135 C VAL A 147 7955 10053 6730 -230 506 1297 C ATOM 1136 O VAL A 147 -25.832 38.734 -6.642 1.00 65.31 O ANISOU 1136 O VAL A 147 7910 10025 6881 -294 478 1191 O ATOM 1137 CB VAL A 147 -24.365 39.895 -9.197 1.00 67.45 C ANISOU 1137 CB VAL A 147 8212 10513 6902 -418 794 1438 C ATOM 1138 CG1 VAL A 147 -23.834 40.637 -7.953 1.00 67.93 C ANISOU 1138 CG1 VAL A 147 8166 10518 7125 -583 833 1343 C ATOM 1139 CG2 VAL A 147 -23.206 39.677 -10.188 1.00 68.58 C ANISOU 1139 CG2 VAL A 147 8306 10868 6881 -428 915 1472 C ATOM 1140 N GLY A 148 -27.457 38.990 -8.210 1.00 64.16 N ANISOU 1140 N GLY A 148 7949 9841 6586 -139 443 1391 N ATOM 1141 CA GLY A 148 -28.602 39.195 -7.313 1.00 56.98 C ANISOU 1141 CA GLY A 148 7082 8766 5803 -108 352 1374 C ATOM 1142 C GLY A 148 -28.800 38.033 -6.317 1.00 52.41 C ANISOU 1142 C GLY A 148 6425 8199 5290 -80 240 1200 C ATOM 1143 O GLY A 148 -28.804 38.303 -5.117 1.00 51.86 O ANISOU 1143 O GLY A 148 6336 8012 5355 -144 230 1142 O ATOM 1144 N PRO A 149 -28.884 36.760 -6.775 1.00 50.81 N ANISOU 1144 N PRO A 149 6194 8126 4984 16 157 1114 N ATOM 1145 CA PRO A 149 -28.766 35.546 -5.939 1.00 48.53 C ANISOU 1145 CA PRO A 149 5863 7829 4748 44 67 957 C ATOM 1146 C PRO A 149 -27.619 35.505 -4.909 1.00 49.34 C ANISOU 1146 C PRO A 149 5885 7932 4929 -30 107 874 C ATOM 1147 O PRO A 149 -27.878 35.151 -3.760 1.00 49.80 O ANISOU 1147 O PRO A 149 5938 7906 5079 -36 50 791 O ATOM 1148 CB PRO A 149 -28.638 34.425 -6.983 1.00 47.09 C ANISOU 1148 CB PRO A 149 5684 7791 4418 141 15 887 C ATOM 1149 CG PRO A 149 -29.520 34.900 -8.124 1.00 47.06 C ANISOU 1149 CG PRO A 149 5737 7843 4302 185 18 1005 C ATOM 1150 CD PRO A 149 -29.270 36.405 -8.144 1.00 49.35 C ANISOU 1150 CD PRO A 149 6044 8079 4626 110 136 1157 C ATOM 1151 N TRP A 150 -26.394 35.883 -5.317 1.00 51.43 N ANISOU 1151 N TRP A 150 6080 8307 5152 -87 205 891 N ATOM 1152 CA TRP A 150 -25.215 35.917 -4.444 1.00 53.44 C ANISOU 1152 CA TRP A 150 6226 8607 5472 -155 233 801 C ATOM 1153 C TRP A 150 -25.269 37.003 -3.355 1.00 57.71 C ANISOU 1153 C TRP A 150 6776 8996 6154 -287 261 824 C ATOM 1154 O TRP A 150 -24.891 36.721 -2.217 1.00 57.71 O ANISOU 1154 O TRP A 150 6725 8974 6227 -312 216 726 O ATOM 1155 CB TRP A 150 -23.928 36.059 -5.278 1.00 52.56 C ANISOU 1155 CB TRP A 150 6008 8685 5277 -192 339 804 C ATOM 1156 CG TRP A 150 -23.565 34.889 -6.142 1.00 50.47 C ANISOU 1156 CG TRP A 150 5722 8580 4875 -47 314 740 C ATOM 1157 CD1 TRP A 150 -23.583 34.857 -7.494 1.00 49.39 C ANISOU 1157 CD1 TRP A 150 5633 8534 4600 10 354 800 C ATOM 1158 CD2 TRP A 150 -23.116 33.567 -5.718 1.00 54.57 C ANISOU 1158 CD2 TRP A 150 6186 9180 5369 72 245 600 C ATOM 1159 CE2 TRP A 150 -22.824 32.793 -6.882 1.00 53.42 C ANISOU 1159 CE2 TRP A 150 6063 9157 5078 194 255 572 C ATOM 1160 CE3 TRP A 150 -22.905 32.948 -4.463 1.00 53.55 C ANISOU 1160 CE3 TRP A 150 6005 9026 5314 100 178 498 C ATOM 1161 NE1 TRP A 150 -23.135 33.628 -7.934 1.00 52.66 N ANISOU 1161 NE1 TRP A 150 6023 9074 4909 147 319 691 N ATOM 1162 CZ2 TRP A 150 -22.316 31.485 -6.806 1.00 46.28 C ANISOU 1162 CZ2 TRP A 150 5142 8329 4113 345 208 445 C ATOM 1163 CZ3 TRP A 150 -22.407 31.633 -4.374 1.00 44.94 C ANISOU 1163 CZ3 TRP A 150 4899 8019 4158 260 126 388 C ATOM 1164 CH2 TRP A 150 -22.099 30.908 -5.542 1.00 45.65 C ANISOU 1164 CH2 TRP A 150 5023 8209 4115 382 146 361 C ATOM 1165 N ILE A 151 -25.743 38.208 -3.711 1.00 57.55 N ANISOU 1165 N ILE A 151 6835 8865 6166 -364 338 953 N ATOM 1166 CA ILE A 151 -25.898 39.341 -2.794 1.00 57.91 C ANISOU 1166 CA ILE A 151 6919 8738 6344 -489 377 969 C ATOM 1167 C ILE A 151 -27.028 39.121 -1.771 1.00 58.49 C ANISOU 1167 C ILE A 151 7048 8677 6496 -422 272 916 C ATOM 1168 O ILE A 151 -26.835 39.443 -0.600 1.00 59.99 O ANISOU 1168 O ILE A 151 7220 8795 6778 -494 260 837 O ATOM 1169 CB ILE A 151 -26.115 40.678 -3.571 1.00 60.67 C ANISOU 1169 CB ILE A 151 7382 8969 6700 -558 492 1132 C ATOM 1170 CG1 ILE A 151 -24.836 41.100 -4.334 1.00 64.58 C ANISOU 1170 CG1 ILE A 151 7823 9601 7113 -652 620 1185 C ATOM 1171 CG2 ILE A 151 -26.669 41.863 -2.744 1.00 60.12 C ANISOU 1171 CG2 ILE A 151 7384 8687 6771 -679 541 1139 C ATOM 1172 CD1 ILE A 151 -23.617 41.437 -3.458 1.00 66.19 C ANISOU 1172 CD1 ILE A 151 7877 9904 7369 -815 678 1072 C ATOM 1173 N LEU A 152 -28.155 38.538 -2.215 1.00 59.25 N ANISOU 1173 N LEU A 152 7208 8755 6551 -292 198 950 N ATOM 1174 CA LEU A 152 -29.290 38.171 -1.366 1.00 59.50 C ANISOU 1174 CA LEU A 152 7275 8684 6650 -237 111 894 C ATOM 1175 C LEU A 152 -28.924 37.080 -0.343 1.00 61.40 C ANISOU 1175 C LEU A 152 7455 8982 6892 -222 44 751 C ATOM 1176 O LEU A 152 -29.330 37.187 0.813 1.00 61.59 O ANISOU 1176 O LEU A 152 7496 8912 6995 -247 15 691 O ATOM 1177 CB LEU A 152 -30.484 37.767 -2.262 1.00 60.13 C ANISOU 1177 CB LEU A 152 7399 8775 6671 -117 44 942 C ATOM 1178 CG LEU A 152 -31.810 37.459 -1.524 1.00 59.63 C ANISOU 1178 CG LEU A 152 7356 8629 6673 -71 -34 885 C ATOM 1179 CD1 LEU A 152 -32.300 38.634 -0.653 1.00 59.08 C ANISOU 1179 CD1 LEU A 152 7329 8392 6727 -120 11 913 C ATOM 1180 CD2 LEU A 152 -32.895 36.994 -2.516 1.00 58.20 C ANISOU 1180 CD2 LEU A 152 7186 8503 6424 28 -101 922 C ATOM 1181 N ALA A 153 -28.121 36.095 -0.768 1.00 61.79 N ANISOU 1181 N ALA A 153 7449 9183 6846 -168 24 700 N ATOM 1182 CA ALA A 153 -27.566 35.052 0.092 1.00 59.12 C ANISOU 1182 CA ALA A 153 7070 8897 6497 -125 -34 579 C ATOM 1183 C ALA A 153 -26.650 35.612 1.195 1.00 59.69 C ANISOU 1183 C ALA A 153 7065 8989 6627 -220 -4 528 C ATOM 1184 O ALA A 153 -26.784 35.241 2.362 1.00 62.11 O ANISOU 1184 O ALA A 153 7367 9279 6954 -197 -61 444 O ATOM 1185 CB ALA A 153 -26.796 34.059 -0.787 1.00 58.56 C ANISOU 1185 CB ALA A 153 6963 8980 6306 -26 -47 536 C ATOM 1186 N LEU A 154 -25.750 36.522 0.805 1.00 57.00 N ANISOU 1186 N LEU A 154 6667 8686 6304 -335 86 577 N ATOM 1187 CA LEU A 154 -24.790 37.188 1.689 1.00 59.75 C ANISOU 1187 CA LEU A 154 6924 9073 6706 -458 116 511 C ATOM 1188 C LEU A 154 -25.461 38.064 2.762 1.00 57.60 C ANISOU 1188 C LEU A 154 6729 8617 6538 -538 107 496 C ATOM 1189 O LEU A 154 -25.007 38.053 3.905 1.00 58.31 O ANISOU 1189 O LEU A 154 6776 8726 6651 -569 62 397 O ATOM 1190 CB LEU A 154 -23.765 37.947 0.811 1.00 66.65 C ANISOU 1190 CB LEU A 154 7723 10029 7572 -592 236 565 C ATOM 1191 CG LEU A 154 -22.586 38.629 1.552 1.00 71.50 C ANISOU 1191 CG LEU A 154 8172 10795 8200 -722 272 472 C ATOM 1192 CD1 LEU A 154 -21.341 38.734 0.640 1.00 74.85 C ANISOU 1192 CD1 LEU A 154 8510 11352 8578 -817 398 529 C ATOM 1193 CD2 LEU A 154 -22.967 40.000 2.162 1.00 72.37 C ANISOU 1193 CD2 LEU A 154 8309 10770 8418 -889 290 429 C ATOM 1194 N VAL A 155 -26.535 38.780 2.387 1.00 53.27 N ANISOU 1194 N VAL A 155 6297 7900 6043 -555 148 593 N ATOM 1195 CA VAL A 155 -27.325 39.631 3.283 1.00 51.71 C ANISOU 1195 CA VAL A 155 6183 7520 5944 -615 156 578 C ATOM 1196 C VAL A 155 -28.073 38.835 4.373 1.00 52.95 C ANISOU 1196 C VAL A 155 6369 7648 6102 -519 60 501 C ATOM 1197 O VAL A 155 -28.114 39.283 5.519 1.00 52.93 O ANISOU 1197 O VAL A 155 6376 7593 6140 -571 44 420 O ATOM 1198 CB VAL A 155 -28.312 40.527 2.471 1.00 49.54 C ANISOU 1198 CB VAL A 155 6027 7079 5716 -610 223 708 C ATOM 1199 CG1 VAL A 155 -29.503 41.122 3.255 1.00 50.31 C ANISOU 1199 CG1 VAL A 155 6218 6990 5907 -616 222 685 C ATOM 1200 CG2 VAL A 155 -27.545 41.670 1.781 1.00 51.49 C ANISOU 1200 CG2 VAL A 155 6285 7307 5974 -741 344 786 C ATOM 1201 N LEU A 156 -28.587 37.654 4.006 1.00 53.19 N ANISOU 1201 N LEU A 156 6422 7712 6077 -389 2 520 N ATOM 1202 CA LEU A 156 -29.277 36.739 4.916 1.00 49.43 C ANISOU 1202 CA LEU A 156 5990 7192 5597 -315 -69 457 C ATOM 1203 C LEU A 156 -28.307 35.948 5.822 1.00 50.72 C ANISOU 1203 C LEU A 156 6110 7448 5713 -297 -123 354 C ATOM 1204 O LEU A 156 -28.751 35.378 6.816 1.00 56.61 O ANISOU 1204 O LEU A 156 6913 8140 6456 -257 -165 304 O ATOM 1205 CB LEU A 156 -30.166 35.788 4.088 1.00 49.87 C ANISOU 1205 CB LEU A 156 6079 7267 5602 -210 -111 488 C ATOM 1206 CG LEU A 156 -31.302 36.476 3.294 1.00 50.86 C ANISOU 1206 CG LEU A 156 6241 7325 5758 -192 -88 583 C ATOM 1207 CD1 LEU A 156 -31.960 35.492 2.308 1.00 49.38 C ANISOU 1207 CD1 LEU A 156 6061 7200 5502 -108 -143 585 C ATOM 1208 CD2 LEU A 156 -32.339 37.177 4.188 1.00 50.84 C ANISOU 1208 CD2 LEU A 156 6288 7179 5850 -213 -67 585 C ATOM 1209 N THR A 157 -27.010 35.941 5.492 1.00 51.92 N ANISOU 1209 N THR A 157 6158 7749 5819 -315 -118 326 N ATOM 1210 CA THR A 157 -25.948 35.294 6.271 1.00 53.27 C ANISOU 1210 CA THR A 157 6266 8041 5933 -270 -178 231 C ATOM 1211 C THR A 157 -25.396 36.205 7.401 1.00 57.17 C ANISOU 1211 C THR A 157 6714 8541 6469 -390 -175 161 C ATOM 1212 O THR A 157 -24.671 35.760 8.290 1.00 60.49 O ANISOU 1212 O THR A 157 7100 9048 6835 -342 -244 79 O ATOM 1213 CB THR A 157 -24.798 34.879 5.314 1.00 54.52 C ANISOU 1213 CB THR A 157 6308 8394 6013 -210 -178 219 C ATOM 1214 CG2 THR A 157 -23.586 34.195 5.966 1.00 53.63 C ANISOU 1214 CG2 THR A 157 6134 8420 5824 -100 -255 128 C ATOM 1215 OG1 THR A 157 -25.328 33.989 4.347 1.00 59.48 O ANISOU 1215 OG1 THR A 157 6996 9008 6596 -112 -174 273 O ATOM 1216 N LEU A 158 -25.768 37.484 7.414 1.00 59.20 N ANISOU 1216 N LEU A 158 6984 8698 6811 -538 -99 190 N ATOM 1217 CA LEU A 158 -25.270 38.467 8.384 1.00 60.36 C ANISOU 1217 CA LEU A 158 7100 8836 6999 -681 -88 106 C ATOM 1218 C LEU A 158 -25.511 38.198 9.894 1.00 58.11 C ANISOU 1218 C LEU A 158 6873 8520 6686 -633 -163 22 C ATOM 1219 O LEU A 158 -24.630 38.580 10.664 1.00 58.95 O ANISOU 1219 O LEU A 158 6900 8737 6761 -697 -204 -82 O ATOM 1220 CB LEU A 158 -25.695 39.901 7.995 1.00 62.83 C ANISOU 1220 CB LEU A 158 7492 8965 7415 -823 17 161 C ATOM 1221 CG LEU A 158 -25.079 40.428 6.677 1.00 66.56 C ANISOU 1221 CG LEU A 158 7906 9474 7909 -937 114 226 C ATOM 1222 CD1 LEU A 158 -25.689 41.789 6.290 1.00 66.57 C ANISOU 1222 CD1 LEU A 158 8042 9245 8006 -1039 221 302 C ATOM 1223 CD2 LEU A 158 -23.537 40.491 6.710 1.00 66.39 C ANISOU 1223 CD2 LEU A 158 7718 9644 7863 -1072 116 122 C ATOM 1224 N PRO A 159 -26.581 37.465 10.298 1.00 56.45 N ANISOU 1224 N PRO A 159 6789 8181 6477 -534 -180 55 N ATOM 1225 CA PRO A 159 -26.709 36.965 11.679 1.00 57.20 C ANISOU 1225 CA PRO A 159 6944 8269 6519 -484 -243 -19 C ATOM 1226 C PRO A 159 -25.600 36.002 12.130 1.00 59.92 C ANISOU 1226 C PRO A 159 7216 8804 6748 -380 -337 -77 C ATOM 1227 O PRO A 159 -25.152 36.138 13.264 1.00 64.15 O ANISOU 1227 O PRO A 159 7745 9404 7226 -384 -393 -162 O ATOM 1228 CB PRO A 159 -28.098 36.303 11.726 1.00 55.68 C ANISOU 1228 CB PRO A 159 6882 7933 6343 -396 -227 44 C ATOM 1229 CG PRO A 159 -28.880 36.994 10.622 1.00 55.82 C ANISOU 1229 CG PRO A 159 6911 7845 6455 -446 -151 127 C ATOM 1230 CD PRO A 159 -27.818 37.214 9.554 1.00 56.04 C ANISOU 1230 CD PRO A 159 6830 7985 6476 -488 -135 154 C ATOM 1231 N VAL A 160 -25.154 35.068 11.271 1.00 57.42 N ANISOU 1231 N VAL A 160 6848 8585 6384 -271 -358 -37 N ATOM 1232 CA VAL A 160 -24.059 34.152 11.614 1.00 57.84 C ANISOU 1232 CA VAL A 160 6829 8824 6324 -137 -443 -88 C ATOM 1233 C VAL A 160 -22.693 34.877 11.636 1.00 62.78 C ANISOU 1233 C VAL A 160 7265 9651 6936 -232 -466 -174 C ATOM 1234 O VAL A 160 -21.886 34.624 12.528 1.00 66.82 O ANISOU 1234 O VAL A 160 7715 10314 7358 -165 -554 -253 O ATOM 1235 CB VAL A 160 -24.039 32.860 10.732 1.00 56.02 C ANISOU 1235 CB VAL A 160 6600 8634 6049 6 -444 -34 C ATOM 1236 CG1 VAL A 160 -24.069 33.068 9.221 1.00 55.98 C ANISOU 1236 CG1 VAL A 160 6515 8827 5929 173 -525 -86 C ATOM 1237 CG2 VAL A 160 -22.879 31.911 11.039 1.00 54.69 C ANISOU 1237 CG2 VAL A 160 6615 8278 5886 76 -430 25 C ATOM 1238 N PHE A 161 -22.494 35.836 10.723 1.00 65.37 N ANISOU 1238 N PHE A 161 7498 9994 7345 -392 -386 -161 N ATOM 1239 CA PHE A 161 -21.328 36.730 10.694 1.00 67.52 C ANISOU 1239 CA PHE A 161 7576 10465 7615 -524 -388 -250 C ATOM 1240 C PHE A 161 -21.128 37.584 11.972 1.00 68.97 C ANISOU 1240 C PHE A 161 7762 10639 7804 -653 -424 -357 C ATOM 1241 O PHE A 161 -19.993 37.853 12.360 1.00 68.19 O ANISOU 1241 O PHE A 161 7494 10759 7655 -711 -481 -469 O ATOM 1242 CB PHE A 161 -21.353 37.527 9.369 1.00 68.40 C ANISOU 1242 CB PHE A 161 7627 10548 7813 -691 -266 -196 C ATOM 1243 CG PHE A 161 -20.609 38.849 9.318 1.00 72.16 C ANISOU 1243 CG PHE A 161 7914 11196 8309 -892 -237 -291 C ATOM 1244 CD1 PHE A 161 -19.221 38.879 9.070 1.00 75.66 C ANISOU 1244 CD1 PHE A 161 8135 11930 8683 -852 -266 -346 C ATOM 1245 CD2 PHE A 161 -21.268 40.041 9.686 1.00 74.44 C ANISOU 1245 CD2 PHE A 161 8246 11353 8685 -1126 -171 -334 C ATOM 1246 CE1 PHE A 161 -18.536 40.086 9.127 1.00 79.56 C ANISOU 1246 CE1 PHE A 161 8427 12606 9196 -1062 -232 -446 C ATOM 1247 CE2 PHE A 161 -20.566 41.236 9.738 1.00 78.49 C ANISOU 1247 CE2 PHE A 161 8587 12016 9219 -1347 -134 -436 C ATOM 1248 CZ PHE A 161 -19.206 41.259 9.454 1.00 80.90 C ANISOU 1248 CZ PHE A 161 8647 12635 9456 -1326 -166 -494 C ATOM 1249 N LEU A 162 -22.240 37.945 12.615 1.00 69.84 N ANISOU 1249 N LEU A 162 8052 10517 7966 -696 -393 -337 N ATOM 1250 CA LEU A 162 -22.336 38.638 13.894 1.00 71.65 C ANISOU 1250 CA LEU A 162 8312 10707 8205 -833 -407 -445 C ATOM 1251 C LEU A 162 -22.314 37.633 15.062 1.00 77.82 C ANISOU 1251 C LEU A 162 9169 11528 8871 -693 -513 -497 C ATOM 1252 O LEU A 162 -21.281 37.502 15.719 1.00 81.01 O ANISOU 1252 O LEU A 162 9505 12066 9208 -754 -583 -622 O ATOM 1253 CB LEU A 162 -23.613 39.515 13.897 1.00 68.44 C ANISOU 1253 CB LEU A 162 8061 10020 7921 -959 -293 -400 C ATOM 1254 CG LEU A 162 -23.548 40.732 12.946 1.00 67.56 C ANISOU 1254 CG LEU A 162 7925 9824 7920 -1108 -173 -335 C ATOM 1255 CD1 LEU A 162 -24.944 41.368 12.764 1.00 66.58 C ANISOU 1255 CD1 LEU A 162 7986 9411 7901 -1164 -73 -278 C ATOM 1256 CD2 LEU A 162 -22.479 41.760 13.376 1.00 69.86 C ANISOU 1256 CD2 LEU A 162 8057 10264 8222 -1320 -155 -445 C ATOM 1257 N PHE A 163 -23.445 36.958 15.287 1.00 78.77 N ANISOU 1257 N PHE A 163 9434 11539 8957 -517 -523 -408 N ATOM 1258 CA PHE A 163 -23.820 36.312 16.543 1.00 79.01 C ANISOU 1258 CA PHE A 163 9593 11540 8887 -409 -585 -435 C ATOM 1259 C PHE A 163 -23.221 34.921 16.790 1.00 77.82 C ANISOU 1259 C PHE A 163 9457 11511 8600 -177 -678 -402 C ATOM 1260 O PHE A 163 -23.288 34.464 17.935 1.00 78.90 O ANISOU 1260 O PHE A 163 9717 11630 8632 -76 -727 -411 O ATOM 1261 CB PHE A 163 -25.358 36.178 16.585 1.00 77.63 C ANISOU 1261 CB PHE A 163 9609 11104 8781 -419 -498 -367 C ATOM 1262 CG PHE A 163 -26.162 37.462 16.495 1.00 79.47 C ANISOU 1262 CG PHE A 163 9860 11186 9147 -603 -398 -384 C ATOM 1263 CD1 PHE A 163 -25.921 38.531 17.384 1.00 81.01 C ANISOU 1263 CD1 PHE A 163 10065 11375 9342 -739 -395 -502 C ATOM 1264 CD2 PHE A 163 -27.246 37.546 15.595 1.00 79.56 C ANISOU 1264 CD2 PHE A 163 9893 11059 9275 -630 -308 -285 C ATOM 1265 CE1 PHE A 163 -26.724 39.662 17.338 1.00 81.73 C ANISOU 1265 CE1 PHE A 163 10203 11295 9556 -895 -292 -519 C ATOM 1266 CE2 PHE A 163 -28.033 38.688 15.563 1.00 80.08 C ANISOU 1266 CE2 PHE A 163 9999 10970 9456 -768 -213 -287 C ATOM 1267 CZ PHE A 163 -27.773 39.741 16.431 1.00 81.00 C ANISOU 1267 CZ PHE A 163 10143 11053 9581 -899 -198 -402 C ATOM 1268 N LEU A 164 -22.722 34.233 15.750 1.00 72.81 N ANISOU 1268 N LEU A 164 8719 10991 7955 -80 -695 -361 N ATOM 1269 CA LEU A 164 -22.161 32.893 15.924 1.00 68.67 C ANISOU 1269 CA LEU A 164 8226 10565 7300 163 -776 -332 C ATOM 1270 C LEU A 164 -20.780 32.961 16.575 1.00 67.32 C ANISOU 1270 C LEU A 164 7867 10693 7019 229 -891 -429 C ATOM 1271 O LEU A 164 -20.001 33.875 16.304 1.00 66.77 O ANISOU 1271 O LEU A 164 7580 10802 6989 146 -888 -480 O ATOM 1272 CB LEU A 164 -22.093 32.120 14.593 1.00 66.52 C ANISOU 1272 CB LEU A 164 7957 10253 7062 259 -731 -248 C ATOM 1273 CG LEU A 164 -21.525 30.681 14.688 1.00 66.06 C ANISOU 1273 CG LEU A 164 8031 10181 6887 513 -782 -200 C ATOM 1274 CD1 LEU A 164 -22.313 29.767 15.639 1.00 63.14 C ANISOU 1274 CD1 LEU A 164 7912 9553 6525 522 -731 -132 C ATOM 1275 CD2 LEU A 164 -21.330 30.035 13.320 1.00 66.35 C ANISOU 1275 CD2 LEU A 164 8002 10283 6925 626 -764 -167 C ATOM 1276 N THR A 165 -20.498 31.947 17.385 1.00 68.03 N ANISOU 1276 N THR A 165 8034 10851 6962 378 -988 -454 N ATOM 1277 CA THR A 165 -19.257 31.845 18.144 1.00 70.42 C ANISOU 1277 CA THR A 165 8157 11465 7134 471 -1121 -550 C ATOM 1278 C THR A 165 -19.192 30.463 18.818 1.00 71.00 C ANISOU 1278 C THR A 165 8377 11569 7030 776 -1213 -495 C ATOM 1279 O THR A 165 -20.235 29.869 19.099 1.00 69.01 O ANISOU 1279 O THR A 165 8375 11078 6768 874 -1159 -390 O ATOM 1280 CB THR A 165 -19.158 32.978 19.218 1.00 70.93 C ANISOU 1280 CB THR A 165 8143 11618 7189 267 -1160 -680 C ATOM 1281 CG2 THR A 165 -20.332 33.018 20.213 1.00 65.67 C ANISOU 1281 CG2 THR A 165 7727 10755 6468 269 -1149 -660 C ATOM 1282 OG1 THR A 165 -17.984 32.874 20.004 1.00 76.24 O ANISOU 1282 OG1 THR A 165 8605 12637 7726 353 -1304 -788 O ATOM 1283 N THR A 166 -17.968 29.987 19.095 1.00 70.58 N ANISOU 1283 N THR A 166 8168 11816 6832 926 -1351 -567 N ATOM 1284 CA THR A 166 -17.734 28.841 19.971 1.00 71.62 C ANISOU 1284 CA THR A 166 8438 12004 6770 1247 -1453 -513 C ATOM 1285 C THR A 166 -18.027 29.242 21.431 1.00 75.34 C ANISOU 1285 C THR A 166 9019 12498 7109 1230 -1528 -557 C ATOM 1286 O THR A 166 -17.420 30.184 21.944 1.00 78.04 O ANISOU 1286 O THR A 166 9171 13062 7420 1092 -1606 -692 O ATOM 1287 CB THR A 166 -16.276 28.323 19.869 1.00 72.00 C ANISOU 1287 CB THR A 166 8247 12393 6715 1474 -1570 -558 C ATOM 1288 CG2 THR A 166 -15.980 27.684 18.508 1.00 70.56 C ANISOU 1288 CG2 THR A 166 8053 12147 6612 1590 -1491 -486 C ATOM 1289 OG1 THR A 166 -15.323 29.342 20.109 1.00 73.54 O ANISOU 1289 OG1 THR A 166 8112 12887 6940 1281 -1626 -709 O ATOM 1290 N VAL A 167 -18.981 28.526 22.043 1.00 74.83 N ANISOU 1290 N VAL A 167 9264 12207 6960 1356 -1496 -450 N ATOM 1291 CA VAL A 167 -19.402 28.694 23.430 1.00 73.00 C ANISOU 1291 CA VAL A 167 9180 11984 6574 1370 -1554 -472 C ATOM 1292 C VAL A 167 -18.984 27.444 24.213 1.00 73.23 C ANISOU 1292 C VAL A 167 9328 12131 6365 1731 -1674 -402 C ATOM 1293 O VAL A 167 -19.153 26.328 23.722 1.00 72.65 O ANISOU 1293 O VAL A 167 9360 11973 6272 1956 -1655 -294 O ATOM 1294 CB VAL A 167 -20.945 28.899 23.566 1.00 70.90 C ANISOU 1294 CB VAL A 167 9186 11372 6381 1219 -1406 -403 C ATOM 1295 CG1 VAL A 167 -21.411 30.077 22.704 1.00 68.53 C ANISOU 1295 CG1 VAL A 167 8777 10947 6316 911 -1287 -455 C ATOM 1296 CG2 VAL A 167 -21.863 27.681 23.322 1.00 70.61 C ANISOU 1296 CG2 VAL A 167 9419 11081 6329 1390 -1322 -243 C ATOM 1297 N THR A 168 -18.441 27.667 25.417 1.00 74.20 N ANISOU 1297 N THR A 168 9445 12453 6296 1794 -1801 -467 N ATOM 1298 CA THR A 168 -17.994 26.611 26.316 1.00 76.96 C ANISOU 1298 CA THR A 168 9929 12929 6385 2153 -1928 -393 C ATOM 1299 C THR A 168 -19.001 26.498 27.470 1.00 78.49 C ANISOU 1299 C THR A 168 10451 12932 6440 2154 -1885 -325 C ATOM 1300 O THR A 168 -19.156 27.437 28.253 1.00 81.80 O ANISOU 1300 O THR A 168 10830 13455 6795 1996 -1926 -432 O ATOM 1301 CB THR A 168 -16.582 26.921 26.882 1.00 79.01 C ANISOU 1301 CB THR A 168 9879 13648 6494 2270 -2137 -528 C ATOM 1302 CG2 THR A 168 -16.066 25.940 27.951 1.00 81.55 C ANISOU 1302 CG2 THR A 168 10349 14105 6530 2688 -2277 -434 C ATOM 1303 OG1 THR A 168 -15.660 26.913 25.808 1.00 78.36 O ANISOU 1303 OG1 THR A 168 9477 13748 6547 2249 -2152 -592 O ATOM 1304 N ILE A 169 -19.655 25.330 27.542 1.00 79.29 N ANISOU 1304 N ILE A 169 10881 12751 6494 2321 -1790 -153 N ATOM 1305 CA ILE A 169 -20.515 24.891 28.645 1.00 81.67 C ANISOU 1305 CA ILE A 169 11530 12849 6654 2342 -1719 -58 C ATOM 1306 C ILE A 169 -19.645 24.639 29.914 1.00 81.99 C ANISOU 1306 C ILE A 169 11584 13177 6391 2560 -1902 -86 C ATOM 1307 O ILE A 169 -18.471 24.308 29.741 1.00 79.84 O ANISOU 1307 O ILE A 169 11078 13234 6024 2749 -2079 -150 O ATOM 1308 CB ILE A 169 -21.225 23.573 28.198 1.00 86.89 C ANISOU 1308 CB ILE A 169 12525 13171 7320 2491 -1585 130 C ATOM 1309 CG1 ILE A 169 -22.455 23.211 29.055 1.00 89.75 C ANISOU 1309 CG1 ILE A 169 13173 13213 7716 2297 -1400 201 C ATOM 1310 CG2 ILE A 169 -20.280 22.362 28.062 1.00 90.09 C ANISOU 1310 CG2 ILE A 169 13101 13659 7469 2900 -1696 242 C ATOM 1311 CD1 ILE A 169 -23.377 22.167 28.407 1.00 92.22 C ANISOU 1311 CD1 ILE A 169 13844 13204 7992 2433 -1270 380 C ATOM 1312 N PRO A 170 -20.183 24.800 31.150 1.00 84.67 N ANISOU 1312 N PRO A 170 12166 13439 6565 2538 -1871 -53 N ATOM 1313 CA PRO A 170 -19.414 24.579 32.401 1.00 90.04 C ANISOU 1313 CA PRO A 170 12880 14408 6922 2774 -2056 -70 C ATOM 1314 C PRO A 170 -18.643 23.252 32.594 1.00 96.15 C ANISOU 1314 C PRO A 170 13666 15237 7630 3127 -2131 41 C ATOM 1315 O PRO A 170 -17.717 23.242 33.404 1.00 97.50 O ANISOU 1315 O PRO A 170 13609 15711 7724 3242 -2287 -44 O ATOM 1316 CB PRO A 170 -20.446 24.804 33.514 1.00 89.55 C ANISOU 1316 CB PRO A 170 13179 14119 6728 2714 -1931 16 C ATOM 1317 CG PRO A 170 -21.403 25.819 32.918 1.00 86.21 C ANISOU 1317 CG PRO A 170 12707 13470 6580 2326 -1747 -57 C ATOM 1318 CD PRO A 170 -21.494 25.382 31.462 1.00 83.88 C ANISOU 1318 CD PRO A 170 12236 13065 6569 2250 -1685 -51 C ATOM 1319 N ASN A 171 -18.991 22.188 31.844 1.00103.24 N ANISOU 1319 N ASN A 171 14822 15845 8558 3298 -2018 216 N ATOM 1320 CA ASN A 171 -18.204 20.951 31.724 1.00112.70 C ANISOU 1320 CA ASN A 171 16029 17079 9711 3644 -2075 303 C ATOM 1321 C ASN A 171 -17.137 21.062 30.603 1.00120.86 C ANISOU 1321 C ASN A 171 16733 18284 10904 3683 -2137 217 C ATOM 1322 O ASN A 171 -16.617 22.153 30.371 1.00118.75 O ANISOU 1322 O ASN A 171 16246 18093 10781 3435 -2132 105 O ATOM 1323 CB ASN A 171 -19.127 19.700 31.668 1.00111.68 C ANISOU 1323 CB ASN A 171 16346 16550 9536 3809 -1917 514 C ATOM 1324 CG ASN A 171 -20.198 19.705 30.571 1.00108.79 C ANISOU 1324 CG ASN A 171 16137 15873 9327 3638 -1753 571 C ATOM 1325 ND2 ASN A 171 -20.033 18.863 29.550 1.00106.14 N ANISOU 1325 ND2 ASN A 171 15725 15495 9110 3754 -1746 584 N ATOM 1326 OD1 ASN A 171 -21.174 20.446 30.656 1.00108.52 O ANISOU 1326 OD1 ASN A 171 16289 15645 9299 3406 -1628 598 O ATOM 1327 N GLY A 172 -16.759 19.934 29.979 1.00133.07 N ANISOU 1327 N GLY A 172 18245 19899 12418 4003 -2187 267 N ATOM 1328 CA GLY A 172 -15.603 19.858 29.079 1.00134.58 C ANISOU 1328 CA GLY A 172 18102 20295 12737 4066 -2244 177 C ATOM 1329 C GLY A 172 -15.907 20.203 27.610 1.00132.92 C ANISOU 1329 C GLY A 172 17981 19837 12687 4013 -2119 233 C ATOM 1330 O GLY A 172 -14.961 20.311 26.830 1.00135.02 O ANISOU 1330 O GLY A 172 18321 20010 12970 4267 -2084 302 O ATOM 1331 N ASP A 173 -17.185 20.345 27.214 1.00118.72 N ANISOU 1331 N ASP A 173 16178 17934 10995 3693 -2049 194 N ATOM 1332 CA ASP A 173 -17.600 20.506 25.810 1.00108.00 C ANISOU 1332 CA ASP A 173 14882 16321 9831 3576 -1907 232 C ATOM 1333 C ASP A 173 -17.381 21.936 25.281 1.00 98.22 C ANISOU 1333 C ASP A 173 13325 15158 8835 3172 -1859 84 C ATOM 1334 O ASP A 173 -17.241 22.882 26.058 1.00 99.29 O ANISOU 1334 O ASP A 173 13425 15304 8996 2908 -1845 16 O ATOM 1335 CB ASP A 173 -19.073 20.097 25.532 1.00106.29 C ANISOU 1335 CB ASP A 173 15107 15643 9635 3507 -1721 379 C ATOM 1336 CG ASP A 173 -19.613 18.888 26.300 1.00106.11 C ANISOU 1336 CG ASP A 173 15436 15444 9435 3893 -1713 543 C ATOM 1337 OD1 ASP A 173 -18.815 17.973 26.600 1.00106.51 O ANISOU 1337 OD1 ASP A 173 15365 15615 9490 4152 -1772 531 O ATOM 1338 OD2 ASP A 173 -20.846 18.863 26.505 1.00105.15 O1- ANISOU 1338 OD2 ASP A 173 15698 15029 9225 3894 -1605 670 O1- ATOM 1339 N THR A 174 -17.426 22.056 23.946 1.00 85.57 N ANISOU 1339 N THR A 174 11515 13595 7403 3135 -1823 39 N ATOM 1340 CA THR A 174 -17.522 23.320 23.220 1.00 78.55 C ANISOU 1340 CA THR A 174 10334 12772 6740 2781 -1768 -84 C ATOM 1341 C THR A 174 -18.478 23.105 22.035 1.00 75.40 C ANISOU 1341 C THR A 174 10083 12018 6546 2600 -1581 -21 C ATOM 1342 O THR A 174 -18.365 22.096 21.341 1.00 72.05 O ANISOU 1342 O THR A 174 9835 11419 6121 2784 -1523 68 O ATOM 1343 CB THR A 174 -16.141 23.795 22.691 1.00 77.58 C ANISOU 1343 CB THR A 174 9814 13024 6639 2856 -1873 -195 C ATOM 1344 CG2 THR A 174 -16.174 24.984 21.713 1.00 74.06 C ANISOU 1344 CG2 THR A 174 9076 12669 6394 2469 -1824 -325 C ATOM 1345 OG1 THR A 174 -15.348 24.183 23.797 1.00 78.51 O ANISOU 1345 OG1 THR A 174 9796 13497 6539 3088 -2064 -248 O ATOM 1346 N TYR A 175 -19.422 24.036 21.881 1.00 72.38 N ANISOU 1346 N TYR A 175 9634 11533 6334 2247 -1490 -74 N ATOM 1347 CA TYR A 175 -20.479 24.031 20.878 1.00 70.95 C ANISOU 1347 CA TYR A 175 9561 11053 6344 2057 -1327 -26 C ATOM 1348 C TYR A 175 -20.351 25.324 20.063 1.00 72.75 C ANISOU 1348 C TYR A 175 9506 11369 6765 1767 -1288 -123 C ATOM 1349 O TYR A 175 -19.970 26.353 20.618 1.00 76.40 O ANISOU 1349 O TYR A 175 9815 11968 7244 1588 -1326 -214 O ATOM 1350 CB TYR A 175 -21.850 23.957 21.592 1.00 68.52 C ANISOU 1350 CB TYR A 175 9555 10442 6037 1934 -1217 49 C ATOM 1351 CG TYR A 175 -22.105 22.650 22.330 1.00 67.75 C ANISOU 1351 CG TYR A 175 9798 10167 5776 2182 -1202 173 C ATOM 1352 CD1 TYR A 175 -22.518 21.515 21.607 1.00 67.82 C ANISOU 1352 CD1 TYR A 175 9976 9981 5811 2315 -1132 250 C ATOM 1353 CD2 TYR A 175 -21.929 22.552 23.728 1.00 66.32 C ANISOU 1353 CD2 TYR A 175 9792 10000 5405 2278 -1247 213 C ATOM 1354 CE1 TYR A 175 -22.723 20.284 22.257 1.00 70.05 C ANISOU 1354 CE1 TYR A 175 10603 10065 5947 2530 -1100 367 C ATOM 1355 CE2 TYR A 175 -22.136 21.318 24.381 1.00 68.39 C ANISOU 1355 CE2 TYR A 175 10398 10078 5509 2504 -1217 343 C ATOM 1356 CZ TYR A 175 -22.508 20.176 23.642 1.00 71.48 C ANISOU 1356 CZ TYR A 175 10963 10254 5942 2625 -1139 422 C ATOM 1357 OH TYR A 175 -22.627 18.957 24.249 1.00 75.72 O ANISOU 1357 OH TYR A 175 11874 10574 6324 2839 -1093 554 O ATOM 1358 N CYS A 176 -20.667 25.265 18.769 1.00 73.85 N ANISOU 1358 N CYS A 176 9599 11422 7040 1723 -1206 -104 N ATOM 1359 CA CYS A 176 -20.686 26.420 17.871 1.00 72.68 C ANISOU 1359 CA CYS A 176 9227 11315 7071 1462 -1146 -166 C ATOM 1360 C CYS A 176 -22.167 26.773 17.678 1.00 67.12 C ANISOU 1360 C CYS A 176 8688 10315 6500 1241 -1016 -118 C ATOM 1361 O CYS A 176 -22.881 26.016 17.022 1.00 66.70 O ANISOU 1361 O CYS A 176 8785 10059 6498 1264 -934 -49 O ATOM 1362 CB CYS A 176 -19.951 26.021 16.571 1.00 75.56 C ANISOU 1362 CB CYS A 176 9443 11785 7483 1556 -1133 -171 C ATOM 1363 SG CYS A 176 -19.905 27.212 15.207 1.00 78.78 S ANISOU 1363 SG CYS A 176 9644 12192 8096 1264 -1028 -206 S ATOM 1364 N THR A 177 -22.644 27.833 18.342 1.00 64.75 N ANISOU 1364 N THR A 177 8355 9996 6252 1031 -997 -164 N ATOM 1365 CA THR A 177 -24.049 28.253 18.408 1.00 66.82 C ANISOU 1365 CA THR A 177 8764 10002 6623 850 -880 -124 C ATOM 1366 C THR A 177 -24.083 29.704 18.944 1.00 66.85 C ANISOU 1366 C THR A 177 8637 10045 6716 616 -861 -205 C ATOM 1367 O THR A 177 -23.080 30.168 19.486 1.00 67.58 O ANISOU 1367 O THR A 177 8527 10349 6802 563 -928 -293 O ATOM 1368 CB THR A 177 -24.862 27.292 19.339 1.00 71.77 C ANISOU 1368 CB THR A 177 9669 10459 7142 941 -855 -58 C ATOM 1369 CG2 THR A 177 -26.261 27.747 19.794 1.00 73.74 C ANISOU 1369 CG2 THR A 177 9934 10857 7228 1017 -952 -104 C ATOM 1370 OG1 THR A 177 -25.069 26.065 18.663 1.00 72.13 O ANISOU 1370 OG1 THR A 177 9818 10291 7298 756 -735 -32 O ATOM 1371 N PHE A 178 -25.197 30.430 18.751 1.00 67.02 N ANISOU 1371 N PHE A 178 8777 9865 6824 472 -762 -182 N ATOM 1372 CA PHE A 178 -25.363 31.808 19.225 1.00 70.30 C ANISOU 1372 CA PHE A 178 9125 10268 7316 271 -729 -256 C ATOM 1373 C PHE A 178 -25.287 31.862 20.766 1.00 79.82 C ANISOU 1373 C PHE A 178 10412 11538 8378 300 -786 -316 C ATOM 1374 O PHE A 178 -26.023 31.139 21.447 1.00 78.67 O ANISOU 1374 O PHE A 178 10466 11282 8142 383 -759 -262 O ATOM 1375 CB PHE A 178 -26.728 32.394 18.792 1.00 68.08 C ANISOU 1375 CB PHE A 178 8930 9760 7176 142 -600 -207 C ATOM 1376 CG PHE A 178 -27.287 31.974 17.442 1.00 66.26 C ANISOU 1376 CG PHE A 178 8634 9474 7067 119 -550 -146 C ATOM 1377 CD1 PHE A 178 -28.098 30.820 17.354 1.00 66.01 C ANISOU 1377 CD1 PHE A 178 8419 9566 7094 70 -572 -172 C ATOM 1378 CD2 PHE A 178 -26.922 32.652 16.257 1.00 64.11 C ANISOU 1378 CD2 PHE A 178 8481 9038 6841 137 -478 -69 C ATOM 1379 CE1 PHE A 178 -28.595 30.413 16.123 1.00 63.99 C ANISOU 1379 CE1 PHE A 178 8116 9269 6927 56 -524 -113 C ATOM 1380 CE2 PHE A 178 -27.443 32.240 15.035 1.00 62.89 C ANISOU 1380 CE2 PHE A 178 8266 8851 6777 118 -444 -23 C ATOM 1381 CZ PHE A 178 -28.280 31.128 14.971 1.00 62.24 C ANISOU 1381 CZ PHE A 178 8017 8890 6739 87 -467 -40 C ATOM 1382 N ASN A 179 -24.430 32.740 21.294 1.00 89.97 N ANISOU 1382 N ASN A 179 11546 13005 9632 219 -860 -433 N ATOM 1383 CA ASN A 179 -24.263 32.936 22.735 1.00 96.18 C ANISOU 1383 CA ASN A 179 12391 13892 10263 239 -933 -513 C ATOM 1384 C ASN A 179 -25.270 33.982 23.245 1.00 97.45 C ANISOU 1384 C ASN A 179 12664 13874 10489 69 -828 -552 C ATOM 1385 O ASN A 179 -24.873 35.074 23.653 1.00 99.21 O ANISOU 1385 O ASN A 179 12806 14139 10750 -96 -829 -673 O ATOM 1386 CB ASN A 179 -22.801 33.324 23.052 1.00 99.81 C ANISOU 1386 CB ASN A 179 12625 14640 10658 206 -1061 -644 C ATOM 1387 CG ASN A 179 -22.403 33.066 24.511 1.00103.36 C ANISOU 1387 CG ASN A 179 13122 15259 10891 298 -1180 -719 C ATOM 1388 ND2 ASN A 179 -21.109 32.950 24.780 1.00105.59 N ANISOU 1388 ND2 ASN A 179 13207 15846 11064 368 -1327 -805 N ATOM 1389 OD1 ASN A 179 -23.239 33.019 25.413 1.00104.16 O ANISOU 1389 OD1 ASN A 179 13427 15236 10913 310 -1140 -702 O ATOM 1390 N PHE A 180 -26.561 33.626 23.213 1.00 94.20 N ANISOU 1390 N PHE A 180 12446 13258 10088 112 -728 -455 N ATOM 1391 CA PHE A 180 -27.697 34.462 23.623 1.00 92.70 C ANISOU 1391 CA PHE A 180 12353 12894 9974 -25 -608 -481 C ATOM 1392 C PHE A 180 -27.543 35.079 25.024 1.00 97.65 C ANISOU 1392 C PHE A 180 13033 13602 10465 -65 -646 -600 C ATOM 1393 O PHE A 180 -27.905 36.236 25.242 1.00 99.48 O ANISOU 1393 O PHE A 180 13255 13765 10776 -219 -583 -692 O ATOM 1394 CB PHE A 180 -28.980 33.609 23.602 1.00 90.35 C ANISOU 1394 CB PHE A 180 12233 12408 9689 34 -498 -363 C ATOM 1395 CG PHE A 180 -29.374 33.047 22.249 1.00 88.05 C ANISOU 1395 CG PHE A 180 11892 12011 9551 25 -440 -273 C ATOM 1396 CD1 PHE A 180 -29.635 33.916 21.170 1.00 86.03 C ANISOU 1396 CD1 PHE A 180 11537 11672 9477 -107 -368 -285 C ATOM 1397 CD2 PHE A 180 -29.546 31.657 22.075 1.00 86.12 C ANISOU 1397 CD2 PHE A 180 11717 11746 9259 155 -457 -177 C ATOM 1398 CE1 PHE A 180 -30.053 33.399 19.953 1.00 83.28 C ANISOU 1398 CE1 PHE A 180 11144 11251 9248 -107 -326 -204 C ATOM 1399 CE2 PHE A 180 -29.954 31.160 20.847 1.00 83.54 C ANISOU 1399 CE2 PHE A 180 11348 11334 9059 138 -409 -112 C ATOM 1400 CZ PHE A 180 -30.203 32.029 19.793 1.00 82.14 C ANISOU 1400 CZ PHE A 180 11057 11103 9051 7 -349 -126 C ATOM 1401 N ALA A 181 -26.950 34.304 25.943 1.00 99.32 N ANISOU 1401 N ALA A 181 13316 13960 10462 83 -750 -601 N ATOM 1402 CA ALA A 181 -26.661 34.732 27.312 1.00 99.46 C ANISOU 1402 CA ALA A 181 13400 14076 10316 60 -797 -714 C ATOM 1403 C ALA A 181 -25.568 35.814 27.437 1.00101.13 C ANISOU 1403 C ALA A 181 13422 14460 10542 -84 -888 -889 C ATOM 1404 O ALA A 181 -25.426 36.367 28.527 1.00104.66 O ANISOU 1404 O ALA A 181 13912 14988 10865 -140 -925 -1016 O ATOM 1405 CB ALA A 181 -26.279 33.487 28.130 1.00 99.12 C ANISOU 1405 CB ALA A 181 13481 14163 10016 280 -899 -656 C ATOM 1406 N SER A 182 -24.829 36.101 26.350 1.00 99.02 N ANISOU 1406 N SER A 182 12953 14252 10418 -160 -915 -907 N ATOM 1407 CA SER A 182 -23.713 37.054 26.328 1.00 99.87 C ANISOU 1407 CA SER A 182 12867 14530 10551 -325 -990 -1074 C ATOM 1408 C SER A 182 -24.009 38.330 25.515 1.00101.73 C ANISOU 1408 C SER A 182 13034 14592 11028 -543 -866 -1099 C ATOM 1409 O SER A 182 -23.123 39.179 25.419 1.00106.60 O ANISOU 1409 O SER A 182 13461 15322 11720 -672 -901 -1175 O ATOM 1410 CB SER A 182 -22.461 36.342 25.784 1.00101.85 C ANISOU 1410 CB SER A 182 12912 15070 10715 -218 -1146 -1087 C ATOM 1411 OG SER A 182 -21.992 35.392 26.719 1.00103.45 O ANISOU 1411 OG SER A 182 13203 15413 10691 29 -1258 -1034 O ATOM 1412 N TRP A 183 -25.228 38.471 24.961 1.00100.41 N ANISOU 1412 N TRP A 183 13016 14155 10978 -580 -716 -1033 N ATOM 1413 CA TRP A 183 -25.669 39.655 24.208 1.00100.82 C ANISOU 1413 CA TRP A 183 13039 14023 11247 -750 -593 -1038 C ATOM 1414 C TRP A 183 -25.900 40.891 25.109 1.00108.76 C ANISOU 1414 C TRP A 183 14121 14936 12266 -918 -536 -1195 C ATOM 1415 O TRP A 183 -25.680 40.831 26.320 1.00112.77 O ANISOU 1415 O TRP A 183 14660 15573 12613 -933 -614 -1326 O ATOM 1416 CB TRP A 183 -26.921 39.305 23.368 1.00 94.70 C ANISOU 1416 CB TRP A 183 12357 13031 10595 -671 -472 -874 C ATOM 1417 CG TRP A 183 -26.788 38.314 22.241 1.00 90.17 C ANISOU 1417 CG TRP A 183 11687 12515 10060 -570 -507 -747 C ATOM 1418 CD1 TRP A 183 -25.720 37.538 21.943 1.00 90.53 C ANISOU 1418 CD1 TRP A 183 11591 12779 10027 -507 -626 -755 C ATOM 1419 CD2 TRP A 183 -27.797 37.983 21.240 1.00 86.60 C ANISOU 1419 CD2 TRP A 183 11265 11913 9726 -516 -422 -605 C ATOM 1420 CE2 TRP A 183 -27.295 36.945 20.400 1.00 85.45 C ANISOU 1420 CE2 TRP A 183 11014 11891 9563 -427 -491 -538 C ATOM 1421 CE3 TRP A 183 -29.095 38.462 20.958 1.00 84.94 C ANISOU 1421 CE3 TRP A 183 11150 11495 9626 -527 -297 -538 C ATOM 1422 NE1 TRP A 183 -26.020 36.719 20.872 1.00 88.45 N ANISOU 1422 NE1 TRP A 183 11288 12493 9826 -414 -611 -628 N ATOM 1423 CZ2 TRP A 183 -28.058 36.387 19.359 1.00 82.51 C ANISOU 1423 CZ2 TRP A 183 10646 11431 9275 -364 -442 -415 C ATOM 1424 CZ3 TRP A 183 -29.872 37.916 19.918 1.00 82.63 C ANISOU 1424 CZ3 TRP A 183 10840 11137 9418 -466 -260 -413 C ATOM 1425 CH2 TRP A 183 -29.357 36.875 19.125 1.00 81.18 C ANISOU 1425 CH2 TRP A 183 10567 11069 9210 -393 -332 -356 C ATOM 1426 N GLY A 184 -26.316 42.011 24.495 1.00112.55 N ANISOU 1426 N GLY A 184 14644 15188 12931 -1035 -399 -1185 N ATOM 1427 CA GLY A 184 -26.560 43.285 25.175 1.00118.72 C ANISOU 1427 CA GLY A 184 15507 15852 13752 -1204 -330 -1341 C ATOM 1428 C GLY A 184 -27.826 43.254 26.048 1.00122.29 C ANISOU 1428 C GLY A 184 16155 16147 14162 -1137 -235 -1357 C ATOM 1429 O GLY A 184 -28.701 42.402 25.882 1.00118.46 O ANISOU 1429 O GLY A 184 15740 15626 13641 -977 -202 -1233 O ATOM 1430 N GLY A 185 -27.913 44.234 26.963 1.00131.18 N ANISOU 1430 N GLY A 185 17371 17180 15292 -1274 -181 -1524 N ATOM 1431 CA GLY A 185 -29.044 44.441 27.868 1.00137.59 C ANISOU 1431 CA GLY A 185 18367 17846 16066 -1223 -73 -1568 C ATOM 1432 C GLY A 185 -28.983 43.518 29.096 1.00143.63 C ANISOU 1432 C GLY A 185 19198 18785 16588 -1116 -154 -1608 C ATOM 1433 O GLY A 185 -28.073 42.703 29.253 1.00145.82 O ANISOU 1433 O GLY A 185 19389 19302 16715 -1076 -308 -1617 O ATOM 1434 N THR A 186 -29.991 43.666 29.968 1.00147.05 N ANISOU 1434 N THR A 186 19795 19098 16978 -1055 -39 -1629 N ATOM 1435 CA THR A 186 -30.248 42.845 31.158 1.00149.46 C ANISOU 1435 CA THR A 186 20202 19537 17048 -944 -78 -1644 C ATOM 1436 C THR A 186 -30.678 41.398 30.780 1.00147.28 C ANISOU 1436 C THR A 186 19898 19338 16724 -777 -115 -1438 C ATOM 1437 O THR A 186 -31.007 41.165 29.618 1.00146.15 O ANISOU 1437 O THR A 186 19675 19109 16746 -744 -78 -1295 O ATOM 1438 CB THR A 186 -31.378 43.497 32.009 1.00151.89 C ANISOU 1438 CB THR A 186 20686 19689 17335 -922 85 -1706 C ATOM 1439 CG2 THR A 186 -31.062 44.937 32.446 1.00153.78 C ANISOU 1439 CG2 THR A 186 20984 19811 17633 -1083 137 -1916 C ATOM 1440 OG1 THR A 186 -32.628 43.473 31.344 1.00150.92 O ANISOU 1440 OG1 THR A 186 20572 19391 17379 -836 232 -1550 O ATOM 1441 N PRO A 187 -30.709 40.445 31.746 1.00145.46 N ANISOU 1441 N PRO A 187 19747 19265 16258 -667 -188 -1421 N ATOM 1442 CA PRO A 187 -31.193 39.069 31.488 1.00142.40 C ANISOU 1442 CA PRO A 187 19383 18901 15822 -510 -194 -1224 C ATOM 1443 C PRO A 187 -32.626 38.936 30.931 1.00138.60 C ANISOU 1443 C PRO A 187 18954 18216 15491 -479 -14 -1098 C ATOM 1444 O PRO A 187 -32.877 37.992 30.182 1.00138.75 O ANISOU 1444 O PRO A 187 18923 18203 15591 -415 -10 -945 O ATOM 1445 CB PRO A 187 -31.036 38.355 32.840 1.00145.40 C ANISOU 1445 CB PRO A 187 19905 19434 15907 -408 -257 -1246 C ATOM 1446 CG PRO A 187 -29.927 39.119 33.541 1.00147.67 C ANISOU 1446 CG PRO A 187 20141 19884 16081 -500 -386 -1449 C ATOM 1447 CD PRO A 187 -30.183 40.557 33.108 1.00147.43 C ANISOU 1447 CD PRO A 187 20064 19691 16261 -680 -289 -1579 C ATOM 1448 N GLU A 188 -33.513 39.893 31.264 1.00134.96 N ANISOU 1448 N GLU A 188 18582 17628 15067 -522 134 -1171 N ATOM 1449 CA GLU A 188 -34.865 40.024 30.707 1.00126.81 C ANISOU 1449 CA GLU A 188 17558 16432 14192 -494 302 -1069 C ATOM 1450 C GLU A 188 -34.836 40.369 29.207 1.00123.08 C ANISOU 1450 C GLU A 188 16937 15863 13966 -532 303 -1005 C ATOM 1451 O GLU A 188 -35.588 39.772 28.435 1.00119.69 O ANISOU 1451 O GLU A 188 16459 15374 13643 -484 362 -870 O ATOM 1452 CB GLU A 188 -35.656 41.040 31.572 1.00124.94 C ANISOU 1452 CB GLU A 188 17425 16095 13952 -518 458 -1182 C ATOM 1453 CG GLU A 188 -37.140 41.299 31.205 1.00122.61 C ANISOU 1453 CG GLU A 188 17100 15655 13831 -483 632 -1100 C ATOM 1454 CD GLU A 188 -37.414 42.254 30.035 1.00124.01 C ANISOU 1454 CD GLU A 188 17257 15682 14180 -524 720 -1200 C ATOM 1455 OE1 GLU A 188 -36.540 43.091 29.722 1.00126.14 O ANISOU 1455 OE1 GLU A 188 17612 15933 14383 -582 718 -1367 O ATOM 1456 OE2 GLU A 188 -38.524 42.147 29.468 1.00123.68 O1- ANISOU 1456 OE2 GLU A 188 17123 15537 14331 -494 789 -1115 O1- ATOM 1457 N GLU A 189 -33.944 41.301 28.832 1.00121.81 N ANISOU 1457 N GLU A 189 16706 15690 13888 -628 242 -1102 N ATOM 1458 CA GLU A 189 -33.709 41.727 27.455 1.00115.28 C ANISOU 1458 CA GLU A 189 15755 14775 13273 -664 246 -1031 C ATOM 1459 C GLU A 189 -33.078 40.626 26.597 1.00109.94 C ANISOU 1459 C GLU A 189 14968 14214 12592 -622 128 -910 C ATOM 1460 O GLU A 189 -33.586 40.385 25.506 1.00109.42 O ANISOU 1460 O GLU A 189 14821 14084 12670 -600 154 -796 O ATOM 1461 CB GLU A 189 -32.880 43.023 27.425 1.00115.08 C ANISOU 1461 CB GLU A 189 15708 14688 13329 -800 234 -1167 C ATOM 1462 CG GLU A 189 -33.624 44.224 28.034 1.00117.34 C ANISOU 1462 CG GLU A 189 16124 14821 13641 -835 365 -1295 C ATOM 1463 CD GLU A 189 -32.713 45.441 28.143 1.00119.66 C ANISOU 1463 CD GLU A 189 16428 15022 14016 -990 364 -1437 C ATOM 1464 OE1 GLU A 189 -32.644 46.200 27.153 1.00119.55 O ANISOU 1464 OE1 GLU A 189 16329 14940 14155 -1045 357 -1372 O ATOM 1465 OE2 GLU A 189 -32.080 45.573 29.214 1.00121.84 O1- ANISOU 1465 OE2 GLU A 189 16807 15290 14196 -1067 375 -1617 O1- ATOM 1466 N ARG A 190 -32.042 39.946 27.122 1.00104.03 N ANISOU 1466 N ARG A 190 14217 13641 11668 -593 -4 -934 N ATOM 1467 CA ARG A 190 -31.372 38.803 26.490 1.00100.14 C ANISOU 1467 CA ARG A 190 13637 13257 11156 -519 -108 -822 C ATOM 1468 C ARG A 190 -32.312 37.623 26.179 1.00 94.49 C ANISOU 1468 C ARG A 190 12977 12470 10454 -416 -39 -670 C ATOM 1469 O ARG A 190 -32.120 36.971 25.154 1.00 91.32 O ANISOU 1469 O ARG A 190 12502 12081 10114 -372 -76 -566 O ATOM 1470 CB ARG A 190 -30.214 38.307 27.377 1.00101.86 C ANISOU 1470 CB ARG A 190 13854 13686 11164 -468 -262 -877 C ATOM 1471 CG ARG A 190 -29.049 39.297 27.526 1.00105.22 C ANISOU 1471 CG ARG A 190 14180 14233 11564 -589 -357 -1042 C ATOM 1472 CD ARG A 190 -27.845 38.634 28.204 1.00107.09 C ANISOU 1472 CD ARG A 190 14358 14728 11602 -503 -535 -1071 C ATOM 1473 NE ARG A 190 -26.804 39.596 28.572 1.00110.48 N ANISOU 1473 NE ARG A 190 14683 15314 11981 -636 -633 -1256 N ATOM 1474 CZ ARG A 190 -26.589 40.123 29.787 1.00113.43 C ANISOU 1474 CZ ARG A 190 15130 15789 12178 -664 -685 -1399 C ATOM 1475 NH1 ARG A 190 -27.347 39.783 30.839 1.00114.32 N1+ ANISOU 1475 NH1 ARG A 190 15433 15860 12144 -556 -638 -1365 N1+ ATOM 1476 NH2 ARG A 190 -25.589 40.998 29.946 1.00115.06 N1+ ANISOU 1476 NH2 ARG A 190 15221 16147 12348 -811 -779 -1584 N1+ ATOM 1477 N LEU A 191 -33.303 37.383 27.056 1.00 92.41 N ANISOU 1477 N LEU A 191 12844 12138 10131 -390 71 -663 N ATOM 1478 CA LEU A 191 -34.290 36.312 26.925 1.00 87.88 C ANISOU 1478 CA LEU A 191 12324 11502 9563 -326 151 -533 C ATOM 1479 C LEU A 191 -35.243 36.520 25.734 1.00 87.77 C ANISOU 1479 C LEU A 191 12211 11374 9764 -360 240 -473 C ATOM 1480 O LEU A 191 -35.458 35.577 24.972 1.00 88.88 O ANISOU 1480 O LEU A 191 12315 11499 9956 -329 239 -368 O ATOM 1481 CB LEU A 191 -35.051 36.166 28.266 1.00 86.28 C ANISOU 1481 CB LEU A 191 12281 11278 9223 -306 257 -548 C ATOM 1482 CG LEU A 191 -36.055 34.992 28.344 1.00 82.06 C ANISOU 1482 CG LEU A 191 11838 10700 8643 -261 340 -422 C ATOM 1483 CD1 LEU A 191 -35.354 33.634 28.153 1.00 81.34 C ANISOU 1483 CD1 LEU A 191 11844 10687 8376 -167 229 -352 C ATOM 1484 CD2 LEU A 191 -36.865 35.041 29.657 1.00 84.33 C ANISOU 1484 CD2 LEU A 191 12239 10940 8863 -282 503 -446 C ATOM 1485 N LYS A 192 -35.798 37.739 25.602 1.00 85.83 N ANISOU 1485 N LYS A 192 11929 11047 9638 -413 315 -543 N ATOM 1486 CA LYS A 192 -36.810 38.057 24.593 1.00 83.84 C ANISOU 1486 CA LYS A 192 11585 10698 9571 -414 397 -482 C ATOM 1487 C LYS A 192 -36.225 38.316 23.193 1.00 80.62 C ANISOU 1487 C LYS A 192 11057 10295 9280 -431 313 -434 C ATOM 1488 O LYS A 192 -36.847 37.887 22.222 1.00 77.33 O ANISOU 1488 O LYS A 192 10561 9846 8973 -408 338 -346 O ATOM 1489 CB LYS A 192 -37.735 39.184 25.102 1.00 88.31 C ANISOU 1489 CB LYS A 192 12176 11163 10213 -427 518 -563 C ATOM 1490 CG LYS A 192 -37.106 40.581 25.262 1.00 92.97 C ANISOU 1490 CG LYS A 192 12805 11723 10798 -490 486 -691 C ATOM 1491 CD LYS A 192 -38.037 41.532 26.032 1.00 97.19 C ANISOU 1491 CD LYS A 192 13405 12136 11389 -482 624 -778 C ATOM 1492 CE LYS A 192 -37.501 42.965 26.153 1.00 99.58 C ANISOU 1492 CE LYS A 192 13766 12374 11696 -567 605 -920 C ATOM 1493 NZ LYS A 192 -38.319 43.764 27.079 1.00101.24 N1+ ANISOU 1493 NZ LYS A 192 14071 12445 11951 -542 750 -1017 N1+ ATOM 1494 N VAL A 193 -35.043 38.954 23.096 1.00 81.03 N ANISOU 1494 N VAL A 193 11084 10403 9300 -479 216 -495 N ATOM 1495 CA VAL A 193 -34.374 39.213 21.811 1.00 78.24 C ANISOU 1495 CA VAL A 193 10616 10075 9038 -502 147 -444 C ATOM 1496 C VAL A 193 -33.800 37.941 21.150 1.00 76.67 C ANISOU 1496 C VAL A 193 10378 9980 8771 -438 59 -360 C ATOM 1497 O VAL A 193 -33.697 37.906 19.925 1.00 78.03 O ANISOU 1497 O VAL A 193 10457 10173 9018 -435 22 -297 O ATOM 1498 CB VAL A 193 -33.225 40.252 21.920 1.00 78.95 C ANISOU 1498 CB VAL A 193 10672 10200 9126 -600 88 -547 C ATOM 1499 CG1 VAL A 193 -33.736 41.630 22.376 1.00 81.77 C ANISOU 1499 CG1 VAL A 193 11100 10419 9550 -669 186 -643 C ATOM 1500 CG2 VAL A 193 -32.008 39.779 22.738 1.00 79.08 C ANISOU 1500 CG2 VAL A 193 10699 10382 8967 -595 -26 -618 C ATOM 1501 N ALA A 194 -33.457 36.918 21.948 1.00 73.60 N ANISOU 1501 N ALA A 194 10079 9649 8236 -379 33 -354 N ATOM 1502 CA ALA A 194 -32.988 35.627 21.447 1.00 72.43 C ANISOU 1502 CA ALA A 194 9932 9565 8022 -299 -35 -272 C ATOM 1503 C ALA A 194 -34.073 34.917 20.621 1.00 72.66 C ANISOU 1503 C ALA A 194 9957 9510 8140 -285 38 -178 C ATOM 1504 O ALA A 194 -33.823 34.511 19.484 1.00 73.25 O ANISOU 1504 O ALA A 194 9976 9607 8247 -255 -7 -117 O ATOM 1505 CB ALA A 194 -32.543 34.767 22.635 1.00 73.46 C ANISOU 1505 CB ALA A 194 10193 9760 7959 -227 -76 -282 C ATOM 1506 N ILE A 195 -35.282 34.853 21.196 1.00 71.01 N ANISOU 1506 N ILE A 195 9797 9219 7965 -310 153 -177 N ATOM 1507 CA ILE A 195 -36.469 34.267 20.580 1.00 73.66 C ANISOU 1507 CA ILE A 195 10104 9503 8380 -315 221 -107 C ATOM 1508 C ILE A 195 -36.862 34.988 19.274 1.00 77.17 C ANISOU 1508 C ILE A 195 10409 9933 8980 -330 217 -80 C ATOM 1509 O ILE A 195 -37.076 34.324 18.260 1.00 79.14 O ANISOU 1509 O ILE A 195 10601 10196 9272 -320 194 -21 O ATOM 1510 CB ILE A 195 -37.683 34.276 21.564 1.00 73.58 C ANISOU 1510 CB ILE A 195 10159 9441 8357 -342 353 -123 C ATOM 1511 CG1 ILE A 195 -37.417 33.436 22.836 1.00 74.14 C ANISOU 1511 CG1 ILE A 195 10395 9519 8254 -323 367 -115 C ATOM 1512 CG2 ILE A 195 -39.048 33.886 20.945 1.00 73.78 C ANISOU 1512 CG2 ILE A 195 10100 9442 8492 -369 426 -74 C ATOM 1513 CD1 ILE A 195 -37.532 31.920 22.628 1.00 72.79 C ANISOU 1513 CD1 ILE A 195 10287 9338 8032 -300 333 -37 C ATOM 1514 N THR A 196 -36.937 36.323 19.303 1.00 78.95 N ANISOU 1514 N THR A 196 10594 10124 9281 -351 242 -124 N ATOM 1515 CA THR A 196 -37.353 37.130 18.149 1.00 80.68 C ANISOU 1515 CA THR A 196 10708 10312 9635 -348 249 -82 C ATOM 1516 C THR A 196 -36.317 37.171 17.003 1.00 79.41 C ANISOU 1516 C THR A 196 10485 10210 9477 -350 152 -42 C ATOM 1517 O THR A 196 -36.738 37.330 15.857 1.00 79.51 O ANISOU 1517 O THR A 196 10421 10228 9562 -331 144 24 O ATOM 1518 CB THR A 196 -37.711 38.587 18.539 1.00 80.78 C ANISOU 1518 CB THR A 196 10733 10239 9719 -363 312 -136 C ATOM 1519 CG2 THR A 196 -38.857 38.690 19.558 1.00 82.04 C ANISOU 1519 CG2 THR A 196 10937 10351 9884 -339 424 -175 C ATOM 1520 OG1 THR A 196 -36.588 39.314 18.996 1.00 82.24 O ANISOU 1520 OG1 THR A 196 10969 10436 9842 -417 265 -216 O ATOM 1521 N MET A 197 -35.021 36.957 17.303 1.00 75.92 N ANISOU 1521 N MET A 197 10066 9833 8949 -365 79 -84 N ATOM 1522 CA MET A 197 -33.968 36.744 16.303 1.00 73.07 C ANISOU 1522 CA MET A 197 9629 9554 8581 -360 -3 -54 C ATOM 1523 C MET A 197 -34.133 35.372 15.632 1.00 70.27 C ANISOU 1523 C MET A 197 9271 9238 8189 -298 -37 11 C ATOM 1524 O MET A 197 -34.182 35.299 14.404 1.00 72.85 O ANISOU 1524 O MET A 197 9525 9594 8560 -286 -59 63 O ATOM 1525 CB MET A 197 -32.562 36.925 16.926 1.00 74.32 C ANISOU 1525 CB MET A 197 9786 9806 8647 -380 -78 -128 C ATOM 1526 CG MET A 197 -31.399 37.087 15.915 1.00 79.80 C ANISOU 1526 CG MET A 197 10368 10598 9355 -403 -139 -120 C ATOM 1527 SD MET A 197 -30.854 35.653 14.927 1.00 82.48 S ANISOU 1527 SD MET A 197 10671 11044 9624 -293 -212 -54 S ATOM 1528 CE MET A 197 -30.206 34.538 16.201 1.00 84.79 C ANISOU 1528 CE MET A 197 11060 11405 9752 -204 -279 -100 C ATOM 1529 N LEU A 198 -34.273 34.310 16.440 1.00 66.66 N ANISOU 1529 N LEU A 198 8910 8774 7643 -263 -33 6 N ATOM 1530 CA LEU A 198 -34.488 32.948 15.941 1.00 64.34 C ANISOU 1530 CA LEU A 198 8647 8484 7314 -219 -50 55 C ATOM 1531 C LEU A 198 -35.784 32.817 15.125 1.00 66.91 C ANISOU 1531 C LEU A 198 8930 8760 7731 -254 11 92 C ATOM 1532 O LEU A 198 -35.783 32.137 14.099 1.00 70.20 O ANISOU 1532 O LEU A 198 9324 9195 8152 -241 -14 124 O ATOM 1533 CB LEU A 198 -34.483 31.942 17.106 1.00 61.52 C ANISOU 1533 CB LEU A 198 8437 8107 6830 -178 -47 49 C ATOM 1534 CG LEU A 198 -33.098 31.690 17.730 1.00 57.96 C ANISOU 1534 CG LEU A 198 8024 7741 6257 -104 -135 20 C ATOM 1535 CD1 LEU A 198 -33.246 30.886 19.037 1.00 56.99 C ANISOU 1535 CD1 LEU A 198 8077 7580 5997 -47 -119 32 C ATOM 1536 CD2 LEU A 198 -32.125 31.022 16.731 1.00 51.83 C ANISOU 1536 CD2 LEU A 198 7178 7049 5468 -34 -218 39 C ATOM 1537 N THR A 199 -36.839 33.523 15.556 1.00 65.45 N ANISOU 1537 N THR A 199 8728 8528 7613 -291 90 78 N ATOM 1538 CA THR A 199 -38.095 33.651 14.823 1.00 63.79 C ANISOU 1538 CA THR A 199 8438 8309 7489 -309 137 107 C ATOM 1539 C THR A 199 -37.882 34.252 13.416 1.00 60.30 C ANISOU 1539 C THR A 199 7887 7905 7120 -285 92 150 C ATOM 1540 O THR A 199 -38.382 33.696 12.438 1.00 61.05 O ANISOU 1540 O THR A 199 7922 8040 7232 -282 71 181 O ATOM 1541 CB THR A 199 -39.128 34.520 15.590 1.00 65.19 C ANISOU 1541 CB THR A 199 8607 8445 7718 -326 235 78 C ATOM 1542 CG2 THR A 199 -40.501 34.655 14.914 1.00 67.00 C ANISOU 1542 CG2 THR A 199 8722 8704 8032 -328 275 102 C ATOM 1543 OG1 THR A 199 -39.362 33.976 16.876 1.00 65.81 O ANISOU 1543 OG1 THR A 199 8799 8495 7711 -354 290 45 O ATOM 1544 N ALA A 200 -37.079 35.325 13.329 1.00 55.18 N ANISOU 1544 N ALA A 200 7219 7244 6503 -278 81 151 N ATOM 1545 CA ALA A 200 -36.695 35.947 12.067 1.00 51.36 C ANISOU 1545 CA ALA A 200 6658 6787 6070 -259 50 207 C ATOM 1546 C ALA A 200 -35.866 35.007 11.178 1.00 55.66 C ANISOU 1546 C ALA A 200 7185 7412 6552 -245 -23 228 C ATOM 1547 O ALA A 200 -36.203 34.869 10.006 1.00 59.80 O ANISOU 1547 O ALA A 200 7649 7982 7092 -222 -47 279 O ATOM 1548 CB ALA A 200 -35.964 37.273 12.324 1.00 48.92 C ANISOU 1548 CB ALA A 200 6358 6427 5801 -284 70 196 C ATOM 1549 N ARG A 201 -34.850 34.333 11.743 1.00 53.23 N ANISOU 1549 N ARG A 201 6935 7131 6160 -242 -61 189 N ATOM 1550 CA ARG A 201 -34.019 33.356 11.023 1.00 50.12 C ANISOU 1550 CA ARG A 201 6532 6812 5699 -203 -124 200 C ATOM 1551 C ARG A 201 -34.845 32.181 10.454 1.00 50.21 C ANISOU 1551 C ARG A 201 6568 6817 5691 -190 -127 211 C ATOM 1552 O ARG A 201 -34.621 31.785 9.311 1.00 49.75 O ANISOU 1552 O ARG A 201 6470 6814 5619 -167 -161 234 O ATOM 1553 CB ARG A 201 -32.833 32.892 11.909 1.00 50.38 C ANISOU 1553 CB ARG A 201 6622 6880 5640 -170 -166 155 C ATOM 1554 CG ARG A 201 -31.815 31.964 11.198 1.00 49.25 C ANISOU 1554 CG ARG A 201 6471 6819 5421 -97 -226 159 C ATOM 1555 CD ARG A 201 -30.547 31.678 12.029 1.00 50.97 C ANISOU 1555 CD ARG A 201 6714 7104 5547 -38 -277 117 C ATOM 1556 NE ARG A 201 -29.686 30.647 11.411 1.00 55.31 N ANISOU 1556 NE ARG A 201 7267 7731 6018 68 -329 118 N ATOM 1557 CZ ARG A 201 -28.671 30.821 10.542 1.00 54.82 C ANISOU 1557 CZ ARG A 201 7087 7789 5952 92 -357 116 C ATOM 1558 NH1 ARG A 201 -28.283 32.033 10.135 1.00 52.77 N1+ ANISOU 1558 NH1 ARG A 201 6712 7573 5765 -2 -334 122 N1+ ATOM 1559 NH2 ARG A 201 -28.016 29.763 10.053 1.00 55.61 N1+ ANISOU 1559 NH2 ARG A 201 7196 7959 5974 211 -395 110 N1+ ATOM 1560 N GLY A 202 -35.820 31.687 11.229 1.00 52.52 N ANISOU 1560 N GLY A 202 6930 7046 5977 -220 -84 188 N ATOM 1561 CA GLY A 202 -36.736 30.622 10.818 1.00 52.37 C ANISOU 1561 CA GLY A 202 6936 7016 5947 -246 -76 183 C ATOM 1562 C GLY A 202 -37.672 31.084 9.691 1.00 51.15 C ANISOU 1562 C GLY A 202 6660 6913 5862 -269 -75 204 C ATOM 1563 O GLY A 202 -37.851 30.369 8.702 1.00 52.15 O ANISOU 1563 O GLY A 202 6770 7079 5967 -282 -105 196 O ATOM 1564 N ILE A 203 -38.227 32.301 9.801 1.00 48.61 N ANISOU 1564 N ILE A 203 6260 6594 5617 -264 -45 228 N ATOM 1565 CA ILE A 203 -39.060 32.920 8.767 1.00 47.94 C ANISOU 1565 CA ILE A 203 6057 6571 5587 -247 -54 263 C ATOM 1566 C ILE A 203 -38.274 33.196 7.469 1.00 49.16 C ANISOU 1566 C ILE A 203 6175 6791 5713 -201 -117 311 C ATOM 1567 O ILE A 203 -38.784 32.900 6.386 1.00 51.49 O ANISOU 1567 O ILE A 203 6414 7165 5984 -193 -158 319 O ATOM 1568 CB ILE A 203 -39.751 34.218 9.289 1.00 45.59 C ANISOU 1568 CB ILE A 203 5709 6241 5373 -219 2 284 C ATOM 1569 CG1 ILE A 203 -40.851 33.851 10.314 1.00 43.34 C ANISOU 1569 CG1 ILE A 203 5440 5921 5107 -264 76 232 C ATOM 1570 CG2 ILE A 203 -40.338 35.151 8.201 1.00 43.41 C ANISOU 1570 CG2 ILE A 203 5318 6036 5138 -157 -21 341 C ATOM 1571 CD1 ILE A 203 -41.328 35.032 11.171 1.00 44.56 C ANISOU 1571 CD1 ILE A 203 5572 6026 5332 -222 146 235 C ATOM 1572 N ILE A 204 -37.041 33.703 7.601 1.00 47.28 N ANISOU 1572 N ILE A 204 5963 6534 5468 -179 -120 335 N ATOM 1573 CA ILE A 204 -36.090 33.894 6.508 1.00 45.72 C ANISOU 1573 CA ILE A 204 5731 6403 5238 -146 -157 385 C ATOM 1574 C ILE A 204 -35.769 32.574 5.787 1.00 47.79 C ANISOU 1574 C ILE A 204 6015 6729 5413 -136 -207 352 C ATOM 1575 O ILE A 204 -35.886 32.524 4.562 1.00 50.18 O ANISOU 1575 O ILE A 204 6278 7112 5677 -109 -240 380 O ATOM 1576 CB ILE A 204 -34.785 34.602 6.995 1.00 42.69 C ANISOU 1576 CB ILE A 204 5360 5993 4865 -158 -136 399 C ATOM 1577 CG1 ILE A 204 -35.027 36.110 7.241 1.00 44.87 C ANISOU 1577 CG1 ILE A 204 5634 6184 5229 -169 -79 432 C ATOM 1578 CG2 ILE A 204 -33.509 34.384 6.149 1.00 40.71 C ANISOU 1578 CG2 ILE A 204 5075 5828 4566 -141 -159 441 C ATOM 1579 CD1 ILE A 204 -35.355 36.932 5.984 1.00 45.07 C ANISOU 1579 CD1 ILE A 204 5683 6169 5273 -220 -49 422 C ATOM 1580 N ARG A 205 -35.448 31.521 6.554 1.00 45.77 N ANISOU 1580 N ARG A 205 5841 6433 5114 -146 -209 292 N ATOM 1581 CA ARG A 205 -35.231 30.173 6.035 1.00 48.15 C ANISOU 1581 CA ARG A 205 6197 6763 5333 -121 -245 254 C ATOM 1582 C ARG A 205 -36.442 29.655 5.231 1.00 49.07 C ANISOU 1582 C ARG A 205 6298 6903 5445 -160 -260 230 C ATOM 1583 O ARG A 205 -36.229 29.103 4.154 1.00 51.12 O ANISOU 1583 O ARG A 205 6561 7222 5641 -139 -296 211 O ATOM 1584 CB ARG A 205 -34.817 29.213 7.182 1.00 46.10 C ANISOU 1584 CB ARG A 205 6058 6428 5027 -107 -237 207 C ATOM 1585 CG ARG A 205 -34.730 27.729 6.760 1.00 46.22 C ANISOU 1585 CG ARG A 205 6170 6433 4961 -68 -260 164 C ATOM 1586 CD ARG A 205 -34.445 26.725 7.879 1.00 48.31 C ANISOU 1586 CD ARG A 205 6590 6591 5175 -44 -240 134 C ATOM 1587 NE ARG A 205 -33.026 26.646 8.234 1.00 53.48 N ANISOU 1587 NE ARG A 205 7248 7272 5800 34 -258 148 N ATOM 1588 CZ ARG A 205 -32.533 26.313 9.435 1.00 51.44 C ANISOU 1588 CZ ARG A 205 7012 6976 5559 9 -235 155 C ATOM 1589 NH1 ARG A 205 -33.324 26.132 10.498 1.00 50.54 N1+ ANISOU 1589 NH1 ARG A 205 6919 6787 5496 -84 -181 155 N1+ ATOM 1590 NH2 ARG A 205 -31.219 26.149 9.583 1.00 48.79 N1+ ANISOU 1590 NH2 ARG A 205 6666 6693 5181 76 -267 152 N1+ ATOM 1591 N PHE A 206 -37.663 29.821 5.761 1.00 47.00 N ANISOU 1591 N PHE A 206 6004 6610 5241 -221 -230 220 N ATOM 1592 CA PHE A 206 -38.860 29.218 5.174 1.00 53.48 C ANISOU 1592 CA PHE A 206 6784 7478 6057 -281 -246 177 C ATOM 1593 C PHE A 206 -39.464 30.053 4.034 1.00 60.83 C ANISOU 1593 C PHE A 206 7581 8534 6997 -242 -291 224 C ATOM 1594 O PHE A 206 -39.627 29.538 2.928 1.00 63.74 O ANISOU 1594 O PHE A 206 7924 8990 7303 -247 -344 195 O ATOM 1595 CB PHE A 206 -39.879 28.866 6.278 1.00 55.99 C ANISOU 1595 CB PHE A 206 7103 7741 6431 -368 -186 139 C ATOM 1596 CG PHE A 206 -41.023 27.984 5.802 1.00 56.75 C ANISOU 1596 CG PHE A 206 7146 7893 6521 -466 -194 72 C ATOM 1597 CD1 PHE A 206 -40.811 26.599 5.654 1.00 55.89 C ANISOU 1597 CD1 PHE A 206 7149 7739 6349 -534 -201 -1 C ATOM 1598 CD2 PHE A 206 -42.226 28.544 5.324 1.00 58.46 C ANISOU 1598 CD2 PHE A 206 7202 8213 6796 -490 -194 71 C ATOM 1599 CE1 PHE A 206 -41.792 25.793 5.092 1.00 56.41 C ANISOU 1599 CE1 PHE A 206 7166 7858 6410 -658 -207 -84 C ATOM 1600 CE2 PHE A 206 -43.196 27.722 4.764 1.00 59.31 C ANISOU 1600 CE2 PHE A 206 7231 8407 6897 -598 -209 -8 C ATOM 1601 CZ PHE A 206 -42.980 26.355 4.647 1.00 59.05 C ANISOU 1601 CZ PHE A 206 7311 8325 6802 -699 -214 -91 C ATOM 1602 N VAL A 207 -39.802 31.326 4.288 1.00 64.35 N ANISOU 1602 N VAL A 207 7956 8985 7508 -195 -271 294 N ATOM 1603 CA VAL A 207 -40.423 32.186 3.279 1.00 64.03 C ANISOU 1603 CA VAL A 207 7806 9053 7470 -132 -309 357 C ATOM 1604 C VAL A 207 -39.436 32.558 2.159 1.00 63.04 C ANISOU 1604 C VAL A 207 7699 8979 7274 -69 -343 419 C ATOM 1605 O VAL A 207 -39.703 32.244 1.001 1.00 66.96 O ANISOU 1605 O VAL A 207 8158 9590 7694 -46 -401 420 O ATOM 1606 CB VAL A 207 -41.038 33.484 3.885 1.00 64.32 C ANISOU 1606 CB VAL A 207 7790 9050 7599 -82 -262 417 C ATOM 1607 CG1 VAL A 207 -41.650 34.439 2.837 1.00 65.70 C ANISOU 1607 CG1 VAL A 207 7863 9334 7766 16 -305 493 C ATOM 1608 CG2 VAL A 207 -42.099 33.153 4.951 1.00 65.18 C ANISOU 1608 CG2 VAL A 207 7877 9121 7769 -146 -211 349 C ATOM 1609 N ILE A 208 -38.287 33.149 2.512 1.00 55.72 N ANISOU 1609 N ILE A 208 6827 7981 6363 -50 -303 465 N ATOM 1610 CA ILE A 208 -37.311 33.610 1.523 1.00 53.44 C ANISOU 1610 CA ILE A 208 6546 7747 6013 -6 -310 529 C ATOM 1611 C ILE A 208 -36.454 32.440 0.997 1.00 56.15 C ANISOU 1611 C ILE A 208 6931 8145 6260 -13 -341 464 C ATOM 1612 O ILE A 208 -36.246 32.344 -0.209 1.00 62.90 O ANISOU 1612 O ILE A 208 7773 9097 7028 25 -365 491 O ATOM 1613 CB ILE A 208 -36.388 34.741 2.077 1.00 50.40 C ANISOU 1613 CB ILE A 208 6189 7278 5683 -13 -247 583 C ATOM 1614 CG1 ILE A 208 -37.186 35.889 2.743 1.00 51.98 C ANISOU 1614 CG1 ILE A 208 6376 7392 5980 3 -206 632 C ATOM 1615 CG2 ILE A 208 -35.409 35.317 1.032 1.00 46.82 C ANISOU 1615 CG2 ILE A 208 5733 6885 5170 11 -232 659 C ATOM 1616 CD1 ILE A 208 -38.164 36.628 1.815 1.00 53.07 C ANISOU 1616 CD1 ILE A 208 6469 7589 6107 87 -227 723 C ATOM 1617 N GLY A 209 -36.008 31.551 1.889 1.00 53.65 N ANISOU 1617 N GLY A 209 6678 7762 5945 -48 -334 380 N ATOM 1618 CA GLY A 209 -35.114 30.444 1.547 1.00 52.30 C ANISOU 1618 CA GLY A 209 6569 7615 5686 -26 -352 318 C ATOM 1619 C GLY A 209 -35.847 29.213 0.993 1.00 52.06 C ANISOU 1619 C GLY A 209 6578 7606 5596 -52 -391 236 C ATOM 1620 O GLY A 209 -35.174 28.245 0.644 1.00 55.00 O ANISOU 1620 O GLY A 209 7016 7997 5884 -17 -403 183 O ATOM 1621 N PHE A 210 -37.188 29.209 0.910 1.00 49.32 N ANISOU 1621 N PHE A 210 6189 7264 5287 -115 -407 214 N ATOM 1622 CA PHE A 210 -37.943 28.086 0.353 1.00 49.94 C ANISOU 1622 CA PHE A 210 6296 7368 5311 -177 -443 115 C ATOM 1623 C PHE A 210 -39.184 28.499 -0.435 1.00 49.90 C ANISOU 1623 C PHE A 210 6163 7495 5301 -201 -496 121 C ATOM 1624 O PHE A 210 -39.212 28.225 -1.635 1.00 48.21 O ANISOU 1624 O PHE A 210 5930 7395 4992 -192 -553 86 O ATOM 1625 CB PHE A 210 -38.140 26.940 1.363 1.00 51.62 C ANISOU 1625 CB PHE A 210 6605 7445 5565 -266 -401 38 C ATOM 1626 CG PHE A 210 -39.110 25.834 0.981 1.00 57.41 C ANISOU 1626 CG PHE A 210 7389 8176 6249 -366 -419 -77 C ATOM 1627 CD1 PHE A 210 -38.746 24.879 0.006 1.00 59.13 C ANISOU 1627 CD1 PHE A 210 7738 8353 6376 -344 -428 -148 C ATOM 1628 CD2 PHE A 210 -40.423 25.828 1.496 1.00 60.82 C ANISOU 1628 CD2 PHE A 210 7735 8649 6727 -487 -423 -127 C ATOM 1629 CE1 PHE A 210 -39.660 23.915 -0.396 1.00 61.64 C ANISOU 1629 CE1 PHE A 210 8125 8647 6649 -455 -438 -271 C ATOM 1630 CE2 PHE A 210 -41.323 24.858 1.077 1.00 64.44 C ANISOU 1630 CE2 PHE A 210 8234 9109 7142 -614 -436 -251 C ATOM 1631 CZ PHE A 210 -40.942 23.906 0.138 1.00 64.54 C ANISOU 1631 CZ PHE A 210 8403 9055 7065 -605 -443 -326 C ATOM 1632 N LEU A 211 -40.174 29.169 0.182 1.00 48.60 N ANISOU 1632 N LEU A 211 5906 7332 5227 -219 -480 161 N ATOM 1633 CA LEU A 211 -41.430 29.495 -0.522 1.00 51.11 C ANISOU 1633 CA LEU A 211 6079 7800 5539 -216 -538 166 C ATOM 1634 C LEU A 211 -41.224 30.347 -1.786 1.00 51.13 C ANISOU 1634 C LEU A 211 6038 7926 5463 -98 -590 261 C ATOM 1635 O LEU A 211 -41.904 30.096 -2.777 1.00 54.26 O ANISOU 1635 O LEU A 211 6354 8483 5779 -83 -669 240 O ATOM 1636 CB LEU A 211 -42.449 30.210 0.393 1.00 56.10 C ANISOU 1636 CB LEU A 211 6618 8411 6284 -217 -499 202 C ATOM 1637 CG LEU A 211 -42.995 29.401 1.587 1.00 59.76 C ANISOU 1637 CG LEU A 211 7091 8804 6813 -349 -445 105 C ATOM 1638 CD1 LEU A 211 -43.868 30.312 2.479 1.00 62.62 C ANISOU 1638 CD1 LEU A 211 7335 9185 7274 -324 -403 143 C ATOM 1639 CD2 LEU A 211 -43.736 28.120 1.147 1.00 59.11 C ANISOU 1639 CD2 LEU A 211 6977 8808 6674 -476 -489 -22 C ATOM 1640 N LEU A 212 -40.284 31.305 -1.732 1.00 47.05 N ANISOU 1640 N LEU A 212 5574 7345 4958 -20 -545 366 N ATOM 1641 CA LEU A 212 -39.889 32.171 -2.841 1.00 49.81 C ANISOU 1641 CA LEU A 212 5906 7793 5226 80 -570 472 C ATOM 1642 C LEU A 212 -39.305 31.379 -4.039 1.00 56.02 C ANISOU 1642 C LEU A 212 6734 8683 5869 82 -615 417 C ATOM 1643 O LEU A 212 -39.938 31.415 -5.095 1.00 60.69 O ANISOU 1643 O LEU A 212 7270 9430 6358 127 -687 430 O ATOM 1644 CB LEU A 212 -38.994 33.309 -2.286 1.00 46.73 C ANISOU 1644 CB LEU A 212 5566 7297 4890 124 -491 585 C ATOM 1645 CG LEU A 212 -38.392 34.272 -3.335 1.00 49.34 C ANISOU 1645 CG LEU A 212 5912 7700 5134 206 -484 706 C ATOM 1646 CD1 LEU A 212 -39.490 35.031 -4.107 1.00 49.95 C ANISOU 1646 CD1 LEU A 212 5925 7866 5185 302 -532 800 C ATOM 1647 CD2 LEU A 212 -37.369 35.226 -2.683 1.00 46.67 C ANISOU 1647 CD2 LEU A 212 5630 7247 4857 195 -390 785 C ATOM 1648 N PRO A 213 -38.169 30.650 -3.894 1.00 55.89 N ANISOU 1648 N PRO A 213 6812 8600 5823 51 -581 349 N ATOM 1649 CA PRO A 213 -37.658 29.815 -4.996 1.00 54.77 C ANISOU 1649 CA PRO A 213 6716 8559 5536 68 -616 286 C ATOM 1650 C PRO A 213 -38.581 28.649 -5.404 1.00 57.88 C ANISOU 1650 C PRO A 213 7100 9019 5874 -6 -690 148 C ATOM 1651 O PRO A 213 -38.659 28.363 -6.598 1.00 60.55 O ANISOU 1651 O PRO A 213 7426 9502 6077 17 -750 115 O ATOM 1652 CB PRO A 213 -36.268 29.352 -4.524 1.00 52.31 C ANISOU 1652 CB PRO A 213 6503 8145 5227 75 -553 244 C ATOM 1653 CG PRO A 213 -36.328 29.430 -3.007 1.00 52.72 C ANISOU 1653 CG PRO A 213 6574 8045 5412 22 -515 229 C ATOM 1654 CD PRO A 213 -37.239 30.630 -2.761 1.00 53.96 C ANISOU 1654 CD PRO A 213 6640 8203 5659 22 -512 329 C ATOM 1655 N MET A 214 -39.311 28.036 -4.457 1.00 58.40 N ANISOU 1655 N MET A 214 7172 8987 6031 -110 -681 60 N ATOM 1656 CA MET A 214 -40.256 26.945 -4.736 1.00 59.51 C ANISOU 1656 CA MET A 214 7304 9182 6125 -222 -737 -88 C ATOM 1657 C MET A 214 -41.438 27.395 -5.609 1.00 58.98 C ANISOU 1657 C MET A 214 7077 9325 6008 -211 -831 -75 C ATOM 1658 O MET A 214 -41.812 26.660 -6.520 1.00 55.87 O ANISOU 1658 O MET A 214 6665 9064 5498 -256 -908 -180 O ATOM 1659 CB MET A 214 -40.737 26.300 -3.416 1.00 61.90 C ANISOU 1659 CB MET A 214 7646 9333 6541 -351 -686 -167 C ATOM 1660 CG MET A 214 -41.653 25.066 -3.533 1.00 66.91 C ANISOU 1660 CG MET A 214 8307 9980 7138 -509 -715 -339 C ATOM 1661 SD MET A 214 -40.833 23.514 -3.999 1.00 71.36 S ANISOU 1661 SD MET A 214 9101 10419 7595 -529 -690 -468 S ATOM 1662 CE MET A 214 -41.060 23.494 -5.798 1.00 71.81 C ANISOU 1662 CE MET A 214 9093 10714 7475 -473 -796 -512 C ATOM 1663 N SER A 215 -41.984 28.595 -5.336 1.00 62.88 N ANISOU 1663 N SER A 215 7456 9856 6580 -142 -832 48 N ATOM 1664 CA SER A 215 -43.050 29.212 -6.129 1.00 66.44 C ANISOU 1664 CA SER A 215 7751 10521 6971 -81 -928 83 C ATOM 1665 C SER A 215 -42.576 29.577 -7.542 1.00 64.91 C ANISOU 1665 C SER A 215 7585 10469 6608 33 -984 147 C ATOM 1666 O SER A 215 -43.302 29.306 -8.494 1.00 66.18 O ANISOU 1666 O SER A 215 7668 10835 6643 38 -1091 89 O ATOM 1667 CB SER A 215 -43.615 30.456 -5.418 1.00 67.90 C ANISOU 1667 CB SER A 215 7840 10687 7271 10 -900 217 C ATOM 1668 OG SER A 215 -44.414 30.075 -4.318 1.00 69.19 O ANISOU 1668 OG SER A 215 7964 10751 7574 -94 -846 151 O ATOM 1669 N ILE A 216 -41.351 30.124 -7.650 1.00 60.66 N ANISOU 1669 N ILE A 216 7154 9840 6055 116 -912 259 N ATOM 1670 CA ILE A 216 -40.678 30.417 -8.916 1.00 60.84 C ANISOU 1670 CA ILE A 216 7217 9991 5910 217 -939 329 C ATOM 1671 C ILE A 216 -40.462 29.151 -9.768 1.00 60.88 C ANISOU 1671 C ILE A 216 7284 10073 5774 151 -982 165 C ATOM 1672 O ILE A 216 -40.858 29.152 -10.930 1.00 61.76 O ANISOU 1672 O ILE A 216 7368 10380 5719 193 -1069 143 O ATOM 1673 CB ILE A 216 -39.326 31.163 -8.688 1.00 60.10 C ANISOU 1673 CB ILE A 216 7213 9778 5845 284 -828 470 C ATOM 1674 CG1 ILE A 216 -39.582 32.616 -8.223 1.00 58.17 C ANISOU 1674 CG1 ILE A 216 6927 9450 5725 346 -785 626 C ATOM 1675 CG2 ILE A 216 -38.370 31.162 -9.900 1.00 64.66 C ANISOU 1675 CG2 ILE A 216 7843 10486 6238 368 -830 534 C ATOM 1676 CD1 ILE A 216 -38.350 33.309 -7.619 1.00 58.63 C ANISOU 1676 CD1 ILE A 216 7066 9364 5845 359 -665 734 C ATOM 1677 N VAL A 217 -39.897 28.094 -9.160 1.00 58.89 N ANISOU 1677 N VAL A 217 7131 9665 5578 58 -924 46 N ATOM 1678 CA VAL A 217 -39.675 26.776 -9.761 1.00 57.92 C ANISOU 1678 CA VAL A 217 7104 9573 5331 5 -947 -119 C ATOM 1679 C VAL A 217 -40.979 26.123 -10.269 1.00 61.72 C ANISOU 1679 C VAL A 217 7510 10189 5753 -105 -1056 -270 C ATOM 1680 O VAL A 217 -41.043 25.759 -11.443 1.00 65.18 O ANISOU 1680 O VAL A 217 7968 10778 6019 -106 -1126 -364 O ATOM 1681 CB VAL A 217 -38.908 25.850 -8.762 1.00 56.35 C ANISOU 1681 CB VAL A 217 7044 9154 5214 -48 -855 -203 C ATOM 1682 CG1 VAL A 217 -39.050 24.326 -8.936 1.00 57.51 C ANISOU 1682 CG1 VAL A 217 7306 9289 5254 -120 -876 -399 C ATOM 1683 CG2 VAL A 217 -37.411 26.206 -8.743 1.00 45.69 C ANISOU 1683 CG2 VAL A 217 5747 7741 3870 67 -765 -87 C ATOM 1684 N ALA A 218 -42.006 26.045 -9.406 1.00 58.94 N ANISOU 1684 N ALA A 218 7061 9801 5532 -206 -1071 -305 N ATOM 1685 CA ALA A 218 -43.314 25.462 -9.718 1.00 59.53 C ANISOU 1685 CA ALA A 218 7037 10018 5564 -343 -1169 -467 C ATOM 1686 C ALA A 218 -44.076 26.181 -10.847 1.00 59.76 C ANISOU 1686 C ALA A 218 6908 10342 5457 -246 -1299 -417 C ATOM 1687 O ALA A 218 -44.640 25.505 -11.707 1.00 58.27 O ANISOU 1687 O ALA A 218 6684 10333 5124 -313 -1401 -562 O ATOM 1688 CB ALA A 218 -44.161 25.415 -8.438 1.00 58.08 C ANISOU 1688 CB ALA A 218 6769 9743 5558 -475 -1134 -508 C ATOM 1689 N ILE A 219 -44.062 27.526 -10.833 1.00 60.46 N ANISOU 1689 N ILE A 219 6914 10480 5577 -83 -1300 -214 N ATOM 1690 CA ILE A 219 -44.733 28.370 -11.825 1.00 61.64 C ANISOU 1690 CA ILE A 219 6919 10903 5597 41 -1425 -141 C ATOM 1691 C ILE A 219 -44.018 28.364 -13.189 1.00 63.56 C ANISOU 1691 C ILE A 219 7258 11275 5616 146 -1465 -106 C ATOM 1692 O ILE A 219 -44.694 28.225 -14.205 1.00 65.33 O ANISOU 1692 O ILE A 219 7403 11756 5663 171 -1597 -169 O ATOM 1693 CB ILE A 219 -44.908 29.835 -11.312 1.00 56.68 C ANISOU 1693 CB ILE A 219 6207 10251 5079 196 -1397 71 C ATOM 1694 CG1 ILE A 219 -45.938 29.878 -10.156 1.00 56.34 C ANISOU 1694 CG1 ILE A 219 6032 10148 5225 98 -1376 11 C ATOM 1695 CG2 ILE A 219 -45.294 30.878 -12.387 1.00 55.54 C ANISOU 1695 CG2 ILE A 219 5961 10365 4776 383 -1515 190 C ATOM 1696 CD1 ILE A 219 -45.891 31.167 -9.321 1.00 56.13 C ANISOU 1696 CD1 ILE A 219 5966 10030 5333 240 -1313 198 C ATOM 1697 N CYS A 220 -42.681 28.504 -13.191 1.00 62.38 N ANISOU 1697 N CYS A 220 7271 10971 5461 207 -1351 -13 N ATOM 1698 CA CYS A 220 -41.857 28.588 -14.400 1.00 64.89 C ANISOU 1698 CA CYS A 220 7679 11413 5563 314 -1362 38 C ATOM 1699 C CYS A 220 -41.856 27.293 -15.224 1.00 69.67 C ANISOU 1699 C CYS A 220 8333 12135 6004 215 -1433 -189 C ATOM 1700 O CYS A 220 -42.071 27.365 -16.433 1.00 73.51 O ANISOU 1700 O CYS A 220 8787 12867 6278 275 -1542 -211 O ATOM 1701 CB CYS A 220 -40.410 28.992 -14.080 1.00 64.50 C ANISOU 1701 CB CYS A 220 7769 11180 5558 371 -1208 159 C ATOM 1702 SG CYS A 220 -40.316 30.772 -13.748 1.00 66.70 S ANISOU 1702 SG CYS A 220 8026 11370 5947 506 -1127 445 S ATOM 1703 N TYR A 221 -41.645 26.141 -14.565 1.00 69.09 N ANISOU 1703 N TYR A 221 8354 11882 6014 69 -1372 -361 N ATOM 1704 CA TYR A 221 -41.678 24.824 -15.210 1.00 71.06 C ANISOU 1704 CA TYR A 221 8681 12201 6117 -36 -1425 -594 C ATOM 1705 C TYR A 221 -43.102 24.359 -15.574 1.00 73.77 C ANISOU 1705 C TYR A 221 8876 12737 6417 -166 -1574 -753 C ATOM 1706 O TYR A 221 -43.236 23.539 -16.483 1.00 76.82 O ANISOU 1706 O TYR A 221 9293 13269 6625 -235 -1657 -934 O ATOM 1707 CB TYR A 221 -40.923 23.797 -14.339 1.00 72.42 C ANISOU 1707 CB TYR A 221 9021 12101 6396 -141 -1310 -726 C ATOM 1708 CG TYR A 221 -39.424 24.049 -14.215 1.00 72.97 C ANISOU 1708 CG TYR A 221 9218 12038 6470 -8 -1178 -609 C ATOM 1709 CD1 TYR A 221 -38.621 24.160 -15.369 1.00 74.11 C ANISOU 1709 CD1 TYR A 221 9442 12303 6413 103 -1163 -602 C ATOM 1710 CD2 TYR A 221 -38.816 24.172 -12.948 1.00 72.01 C ANISOU 1710 CD2 TYR A 221 9125 11692 6543 5 -1069 -514 C ATOM 1711 CE1 TYR A 221 -37.245 24.428 -15.259 1.00 73.66 C ANISOU 1711 CE1 TYR A 221 9470 12155 6361 216 -1035 -504 C ATOM 1712 CE2 TYR A 221 -37.439 24.437 -12.832 1.00 70.72 C ANISOU 1712 CE2 TYR A 221 9046 11444 6382 118 -957 -421 C ATOM 1713 CZ TYR A 221 -36.652 24.570 -13.991 1.00 72.42 C ANISOU 1713 CZ TYR A 221 9319 11789 6407 220 -938 -417 C ATOM 1714 OH TYR A 221 -35.319 24.831 -13.887 1.00 74.50 O ANISOU 1714 OH TYR A 221 9638 11996 6674 323 -819 -333 O ATOM 1715 N GLY A 222 -44.131 24.924 -14.915 1.00 73.61 N ANISOU 1715 N GLY A 222 8686 12735 6549 -203 -1608 -701 N ATOM 1716 CA GLY A 222 -45.540 24.709 -15.246 1.00 73.10 C ANISOU 1716 CA GLY A 222 8424 12923 6427 -296 -1760 -827 C ATOM 1717 C GLY A 222 -45.954 25.529 -16.480 1.00 72.78 C ANISOU 1717 C GLY A 222 8273 13206 6173 -115 -1900 -726 C ATOM 1718 O GLY A 222 -46.730 25.035 -17.297 1.00 74.76 O ANISOU 1718 O GLY A 222 8414 13726 6267 -178 -2050 -881 O ATOM 1719 N LEU A 223 -45.415 26.752 -16.639 1.00 70.24 N ANISOU 1719 N LEU A 223 7987 12867 5834 108 -1853 -466 N ATOM 1720 CA LEU A 223 -45.614 27.617 -17.807 1.00 72.44 C ANISOU 1720 CA LEU A 223 8215 13424 5883 306 -1967 -339 C ATOM 1721 C LEU A 223 -44.892 27.094 -19.059 1.00 72.84 C ANISOU 1721 C LEU A 223 8413 13583 5681 309 -1991 -439 C ATOM 1722 O LEU A 223 -45.427 27.246 -20.156 1.00 76.51 O ANISOU 1722 O LEU A 223 8813 14350 5907 377 -2139 -476 O ATOM 1723 CB LEU A 223 -45.146 29.053 -17.484 1.00 71.75 C ANISOU 1723 CB LEU A 223 8170 13239 5852 522 -1879 -32 C ATOM 1724 CG LEU A 223 -46.153 29.894 -16.672 1.00 72.07 C ANISOU 1724 CG LEU A 223 8064 13223 6098 581 -1873 93 C ATOM 1725 CD1 LEU A 223 -45.494 31.188 -16.157 1.00 70.69 C ANISOU 1725 CD1 LEU A 223 8003 12840 6017 735 -1733 360 C ATOM 1726 CD2 LEU A 223 -47.446 30.189 -17.461 1.00 72.70 C ANISOU 1726 CD2 LEU A 223 7931 13631 6060 695 -2057 104 C ATOM 1727 N ILE A 224 -43.716 26.469 -18.876 1.00 68.70 N ANISOU 1727 N ILE A 224 8083 12828 5192 251 -1847 -487 N ATOM 1728 CA ILE A 224 -42.960 25.784 -19.927 1.00 69.74 C ANISOU 1728 CA ILE A 224 8364 13046 5090 256 -1849 -603 C ATOM 1729 C ILE A 224 -43.705 24.545 -20.462 1.00 75.16 C ANISOU 1729 C ILE A 224 9015 13867 5676 68 -1974 -912 C ATOM 1730 O ILE A 224 -43.740 24.353 -21.677 1.00 80.54 O ANISOU 1730 O ILE A 224 9707 14801 6094 97 -2084 -1008 O ATOM 1731 CB ILE A 224 -41.533 25.397 -19.432 1.00 68.22 C ANISOU 1731 CB ILE A 224 8366 12575 4978 253 -1659 -591 C ATOM 1732 CG1 ILE A 224 -40.657 26.664 -19.311 1.00 66.37 C ANISOU 1732 CG1 ILE A 224 8154 12239 4823 414 -1539 -299 C ATOM 1733 CG2 ILE A 224 -40.790 24.322 -20.262 1.00 69.00 C ANISOU 1733 CG2 ILE A 224 8619 12760 4838 261 -1649 -739 C ATOM 1734 CD1 ILE A 224 -39.401 26.485 -18.446 1.00 63.71 C ANISOU 1734 CD1 ILE A 224 7961 11659 4586 412 -1359 -284 C ATOM 1735 N ALA A 225 -44.322 23.767 -19.553 1.00 74.83 N ANISOU 1735 N ALA A 225 8939 13658 5834 -139 -1952 -1075 N ATOM 1736 CA ALA A 225 -45.175 22.622 -19.875 1.00 76.46 C ANISOU 1736 CA ALA A 225 9121 13963 5969 -363 -2053 -1382 C ATOM 1737 C ALA A 225 -46.470 23.021 -20.605 1.00 80.72 C ANISOU 1737 C ALA A 225 9421 14890 6358 -360 -2264 -1430 C ATOM 1738 O ALA A 225 -46.871 22.318 -21.531 1.00 84.97 O ANISOU 1738 O ALA A 225 9946 15625 6714 -484 -2383 -1668 O ATOM 1739 CB ALA A 225 -45.497 21.855 -18.584 1.00 73.85 C ANISOU 1739 CB ALA A 225 8803 13362 5896 -590 -1967 -1513 C ATOM 1740 N ALA A 226 -47.077 24.150 -20.198 1.00 84.28 N ANISOU 1740 N ALA A 226 9683 15461 6878 -211 -2316 -1215 N ATOM 1741 CA ALA A 226 -48.284 24.718 -20.802 1.00 89.71 C ANISOU 1741 CA ALA A 226 10130 16547 7410 -153 -2525 -1234 C ATOM 1742 C ALA A 226 -48.048 25.298 -22.207 1.00 91.47 C ANISOU 1742 C ALA A 226 10424 16969 7361 69 -2593 -1116 C ATOM 1743 O ALA A 226 -48.924 25.161 -23.058 1.00 97.56 O ANISOU 1743 O ALA A 226 11098 17953 8016 68 -2722 -1206 O ATOM 1744 CB ALA A 226 -48.863 25.787 -19.864 1.00 72.89 C ANISOU 1744 CB ALA A 226 7787 14447 5461 -40 -2541 -1039 C ATOM 1745 N LYS A 227 -46.869 25.906 -22.430 1.00 88.53 N ANISOU 1745 N LYS A 227 10233 16485 6918 251 -2480 -904 N ATOM 1746 CA LYS A 227 -46.431 26.449 -23.718 1.00 92.99 C ANISOU 1746 CA LYS A 227 10906 17163 7263 444 -2491 -775 C ATOM 1747 C LYS A 227 -46.093 25.343 -24.738 1.00 99.77 C ANISOU 1747 C LYS A 227 11900 18062 7945 319 -2509 -1027 C ATOM 1748 O LYS A 227 -46.402 25.505 -25.919 1.00106.28 O ANISOU 1748 O LYS A 227 12725 19073 8582 396 -2599 -1038 O ATOM 1749 CB LYS A 227 -45.256 27.417 -23.460 1.00 87.14 C ANISOU 1749 CB LYS A 227 10326 16275 6510 632 -2335 -496 C ATOM 1750 CG LYS A 227 -44.629 28.096 -24.694 1.00 85.59 C ANISOU 1750 CG LYS A 227 10251 16178 6093 826 -2317 -331 C ATOM 1751 CD LYS A 227 -45.592 28.985 -25.496 1.00 85.17 C ANISOU 1751 CD LYS A 227 10068 16292 6001 1010 -2428 -143 C ATOM 1752 CE LYS A 227 -44.868 29.734 -26.625 1.00 89.88 C ANISOU 1752 CE LYS A 227 10817 16955 6378 1206 -2387 51 C ATOM 1753 NZ LYS A 227 -45.787 30.609 -27.370 1.00 94.10 N1+ ANISOU 1753 NZ LYS A 227 11255 17633 6865 1410 -2487 247 N1+ ATOM 1754 N ILE A 228 -45.515 24.228 -24.252 1.00103.16 N ANISOU 1754 N ILE A 228 12458 18312 8425 135 -2422 -1233 N ATOM 1755 CA ILE A 228 -45.286 22.992 -25.007 1.00105.59 C ANISOU 1755 CA ILE A 228 12912 18625 8580 7 -2431 -1499 C ATOM 1756 C ILE A 228 -46.602 22.304 -25.429 1.00111.12 C ANISOU 1756 C ILE A 228 13460 19485 9275 -180 -2593 -1738 C ATOM 1757 O ILE A 228 -46.684 21.825 -26.558 1.00115.18 O ANISOU 1757 O ILE A 228 14029 20126 9608 -210 -2666 -1884 O ATOM 1758 CB ILE A 228 -44.387 22.002 -24.194 1.00102.75 C ANISOU 1758 CB ILE A 228 12746 18003 8290 -123 -2285 -1657 C ATOM 1759 CG1 ILE A 228 -42.912 22.467 -24.227 1.00 96.99 C ANISOU 1759 CG1 ILE A 228 12143 17088 7621 66 -2104 -1398 C ATOM 1760 CG2 ILE A 228 -44.481 20.508 -24.586 1.00105.64 C ANISOU 1760 CG2 ILE A 228 13295 18345 8499 -234 -2279 -1933 C ATOM 1761 CD1 ILE A 228 -42.034 21.844 -23.129 1.00 93.85 C ANISOU 1761 CD1 ILE A 228 11930 16325 7404 -21 -1919 -1491 C ATOM 1762 N HIS A 229 -47.598 22.293 -24.525 1.00113.57 N ANISOU 1762 N HIS A 229 13568 19800 9782 -314 -2646 -1784 N ATOM 1763 CA HIS A 229 -48.932 21.726 -24.746 1.00120.46 C ANISOU 1763 CA HIS A 229 14256 20844 10669 -501 -2789 -2000 C ATOM 1764 C HIS A 229 -49.791 22.568 -25.712 1.00125.84 C ANISOU 1764 C HIS A 229 14776 21834 11205 -314 -2939 -1878 C ATOM 1765 O HIS A 229 -50.594 21.996 -26.448 1.00128.58 O ANISOU 1765 O HIS A 229 15013 22365 11475 -436 -3066 -2072 O ATOM 1766 CB HIS A 229 -49.610 21.537 -23.372 1.00121.61 C ANISOU 1766 CB HIS A 229 14208 20929 11069 -677 -2785 -2052 C ATOM 1767 CG HIS A 229 -50.910 20.768 -23.373 1.00126.32 C ANISOU 1767 CG HIS A 229 14636 21648 11712 -942 -2886 -2321 C ATOM 1768 CD2 HIS A 229 -51.190 19.454 -23.067 1.00127.77 C ANISOU 1768 CD2 HIS A 229 14847 21681 12018 -1273 -2839 -2594 C ATOM 1769 ND1 HIS A 229 -52.133 21.343 -23.680 1.00130.39 N ANISOU 1769 ND1 HIS A 229 14926 22473 12144 -882 -3045 -2325 N ATOM 1770 CE1 HIS A 229 -53.059 20.388 -23.569 1.00132.65 C ANISOU 1770 CE1 HIS A 229 15088 22812 12499 -1172 -3095 -2593 C ATOM 1771 NE2 HIS A 229 -52.559 19.215 -23.199 1.00131.21 N ANISOU 1771 NE2 HIS A 229 15065 22342 12448 -1421 -2966 -2757 N ATOM 1772 N LYS A 230 -49.594 23.898 -25.705 1.00129.14 N ANISOU 1772 N LYS A 230 15187 22301 11578 -22 -2922 -1561 N ATOM 1773 CA LYS A 230 -50.272 24.861 -26.579 1.00135.91 C ANISOU 1773 CA LYS A 230 15916 23430 12293 183 -3055 -1423 C ATOM 1774 C LYS A 230 -49.817 24.787 -28.053 1.00140.83 C ANISOU 1774 C LYS A 230 16698 24168 12641 232 -3097 -1493 C ATOM 1775 O LYS A 230 -50.561 25.233 -28.926 1.00143.89 O ANISOU 1775 O LYS A 230 16988 24774 12911 156 -3240 -1667 O ATOM 1776 CB LYS A 230 -50.099 26.272 -25.968 1.00133.80 C ANISOU 1776 CB LYS A 230 15638 23130 12071 472 -3000 -1059 C ATOM 1777 CG LYS A 230 -50.793 27.415 -26.733 1.00138.24 C ANISOU 1777 CG LYS A 230 16057 23947 12522 702 -3132 -896 C ATOM 1778 CD LYS A 230 -50.787 28.740 -25.958 1.00137.25 C ANISOU 1778 CD LYS A 230 15961 23731 12456 978 -3054 -540 C ATOM 1779 CE LYS A 230 -51.501 29.863 -26.724 1.00142.58 C ANISOU 1779 CE LYS A 230 16501 24642 13033 1219 -3183 -382 C ATOM 1780 NZ LYS A 230 -51.531 31.113 -25.945 1.00142.99 N1+ ANISOU 1780 NZ LYS A 230 16625 24570 13136 1491 -3093 -32 N1+ ATOM 1781 N LYS A 231 -48.627 24.215 -28.302 1.00143.44 N ANISOU 1781 N LYS A 231 17272 24366 12864 355 -2967 -1362 N ATOM 1782 CA LYS A 231 -48.048 24.023 -29.630 1.00151.14 C ANISOU 1782 CA LYS A 231 18418 25436 13573 406 -2980 -1422 C ATOM 1783 C LYS A 231 -47.686 22.533 -29.810 1.00156.90 C ANISOU 1783 C LYS A 231 19280 26060 14275 151 -2952 -1762 C ATOM 1784 O LYS A 231 -48.249 21.680 -29.123 1.00157.51 O ANISOU 1784 O LYS A 231 19285 26032 14528 -79 -2957 -1963 O ATOM 1785 CB LYS A 231 -46.858 25.013 -29.776 1.00147.64 C ANISOU 1785 CB LYS A 231 18173 24893 13030 631 -2829 -1147 C ATOM 1786 CG LYS A 231 -46.367 25.334 -31.206 1.00147.89 C ANISOU 1786 CG LYS A 231 18314 25107 12772 785 -2868 -1076 C ATOM 1787 CD LYS A 231 -47.460 25.893 -32.138 1.00145.81 C ANISOU 1787 CD LYS A 231 17867 25110 12425 920 -3048 -976 C ATOM 1788 CE LYS A 231 -46.927 26.405 -33.485 1.00144.93 C ANISOU 1788 CE LYS A 231 17886 25167 12016 1097 -3074 -865 C ATOM 1789 NZ LYS A 231 -46.392 25.314 -34.319 1.00145.34 N1+ ANISOU 1789 NZ LYS A 231 18071 25275 11876 955 -3092 -1138 N1+ ATOM 1790 N GLY A 232 -46.778 22.235 -30.751 1.00161.66 N ANISOU 1790 N GLY A 232 20090 26676 14658 188 -2912 -1829 N ATOM 1791 CA GLY A 232 -46.246 20.895 -30.984 1.00166.36 C ANISOU 1791 CA GLY A 232 20854 27141 15213 -24 -2867 -2145 C ATOM 1792 C GLY A 232 -45.057 20.620 -30.051 1.00167.74 C ANISOU 1792 C GLY A 232 21195 27006 15532 -72 -2674 -2159 C ATOM 1793 O GLY A 232 -44.550 21.513 -29.367 1.00166.38 O ANISOU 1793 O GLY A 232 20946 26718 15554 -32 -2608 -1992 O ATOM 1794 N MET A 233 -44.592 19.361 -30.066 1.00170.98 N ANISOU 1794 N MET A 233 21839 27281 15843 -146 -2581 -2360 N ATOM 1795 CA MET A 233 -43.497 18.841 -29.240 1.00171.38 C ANISOU 1795 CA MET A 233 22069 27044 16005 -169 -2394 -2397 C ATOM 1796 C MET A 233 -42.089 19.107 -29.825 1.00173.14 C ANISOU 1796 C MET A 233 22474 27241 16070 46 -2241 -2246 C ATOM 1797 O MET A 233 -41.168 18.341 -29.543 1.00174.55 O ANISOU 1797 O MET A 233 22859 27241 16222 33 -2101 -2381 O ATOM 1798 CB MET A 233 -43.748 17.339 -28.969 1.00173.87 C ANISOU 1798 CB MET A 233 22526 27174 16362 -422 -2377 -2760 C ATOM 1799 CG MET A 233 -45.058 17.059 -28.212 1.00174.49 C ANISOU 1799 CG MET A 233 22451 27175 16673 -663 -2446 -2887 C ATOM 1800 SD MET A 233 -45.330 15.316 -27.789 1.00178.10 S ANISOU 1800 SD MET A 233 23064 27453 17152 -999 -2459 -3324 S ATOM 1801 CE MET A 233 -45.712 14.633 -29.424 1.00182.62 C ANISOU 1801 CE MET A 233 23522 28366 17499 -1031 -2666 -3434 C ATOM 1802 N ILE A 234 -41.933 20.189 -30.611 1.00167.45 N ANISOU 1802 N ILE A 234 21682 26694 15246 252 -2254 -1962 N ATOM 1803 CA ILE A 234 -40.683 20.607 -31.256 1.00163.56 C ANISOU 1803 CA ILE A 234 21341 26188 14614 443 -2092 -1794 C ATOM 1804 C ILE A 234 -39.590 20.982 -30.230 1.00158.62 C ANISOU 1804 C ILE A 234 20746 25356 14168 506 -1913 -1643 C ATOM 1805 O ILE A 234 -38.464 20.498 -30.351 1.00156.09 O ANISOU 1805 O ILE A 234 20583 24925 13798 570 -1742 -1665 O ATOM 1806 CB ILE A 234 -40.909 21.785 -32.265 1.00164.24 C ANISOU 1806 CB ILE A 234 21362 26505 14537 626 -2151 -1533 C ATOM 1807 CG1 ILE A 234 -41.712 21.331 -33.512 1.00166.11 C ANISOU 1807 CG1 ILE A 234 21694 26926 14495 627 -2231 -1683 C ATOM 1808 CG2 ILE A 234 -39.609 22.470 -32.751 1.00163.72 C ANISOU 1808 CG2 ILE A 234 21362 26379 14467 814 -1965 -1229 C ATOM 1809 CD1 ILE A 234 -43.204 21.057 -33.273 1.00167.63 C ANISOU 1809 CD1 ILE A 234 21799 27223 14671 441 -2433 -1961 C ATOM 1810 N LYS A 235 -39.955 21.794 -29.221 1.00162.50 N ANISOU 1810 N LYS A 235 21078 25798 14866 493 -1947 -1497 N ATOM 1811 CA LYS A 235 -39.090 22.135 -28.086 1.00163.10 C ANISOU 1811 CA LYS A 235 21169 25678 15123 528 -1797 -1378 C ATOM 1812 C LYS A 235 -38.935 20.964 -27.093 1.00176.65 C ANISOU 1812 C LYS A 235 22945 27190 16985 355 -1769 -1639 C ATOM 1813 O LYS A 235 -37.909 20.881 -26.416 1.00178.70 O ANISOU 1813 O LYS A 235 23258 27265 17374 389 -1627 -1586 O ATOM 1814 CB LYS A 235 -39.620 23.429 -27.418 1.00151.47 C ANISOU 1814 CB LYS A 235 19520 24231 13803 596 -1837 -1100 C ATOM 1815 CG LYS A 235 -38.750 23.980 -26.266 1.00139.68 C ANISOU 1815 CG LYS A 235 18062 22631 12378 737 -1659 -830 C ATOM 1816 CD LYS A 235 -39.149 23.484 -24.862 1.00131.32 C ANISOU 1816 CD LYS A 235 17016 21300 11579 652 -1549 -880 C ATOM 1817 CE LYS A 235 -37.958 23.449 -23.891 1.00125.32 C ANISOU 1817 CE LYS A 235 16339 20392 10884 762 -1331 -703 C ATOM 1818 NZ LYS A 235 -38.378 23.052 -22.537 1.00120.69 N1+ ANISOU 1818 NZ LYS A 235 15812 19505 10540 683 -1210 -822 N1+ ATOM 1819 N SER A 236 -39.945 20.079 -27.043 1.00186.34 N ANISOU 1819 N SER A 236 24173 28424 18205 165 -1889 -1916 N ATOM 1820 CA SER A 236 -40.041 18.924 -26.151 1.00186.30 C ANISOU 1820 CA SER A 236 24264 28193 18328 -19 -1848 -2180 C ATOM 1821 C SER A 236 -39.307 17.673 -26.690 1.00187.55 C ANISOU 1821 C SER A 236 24679 28199 18380 21 -1703 -2356 C ATOM 1822 O SER A 236 -39.740 16.550 -26.430 1.00189.46 O ANISOU 1822 O SER A 236 25060 28294 18632 -143 -1704 -2648 O ATOM 1823 CB SER A 236 -41.535 18.692 -25.847 1.00188.16 C ANISOU 1823 CB SER A 236 24413 28476 18603 -262 -2011 -2414 C ATOM 1824 OG SER A 236 -41.735 17.779 -24.791 1.00 0.00 O ATOM 1825 N SER A 237 -38.175 17.886 -27.386 1.00182.14 N ANISOU 1825 N SER A 237 24068 27537 17600 235 -1564 -2186 N ATOM 1826 CA SER A 237 -37.198 16.857 -27.760 1.00180.18 C ANISOU 1826 CA SER A 237 24046 27160 17253 305 -1414 -2346 C ATOM 1827 C SER A 237 -36.491 16.236 -26.530 1.00172.94 C ANISOU 1827 C SER A 237 23235 25887 16588 267 -1282 -2422 C ATOM 1828 O SER A 237 -35.990 15.116 -26.618 1.00174.85 O ANISOU 1828 O SER A 237 23688 25961 16785 273 -1189 -2641 O ATOM 1829 CB SER A 237 -36.191 17.492 -28.743 1.00183.73 C ANISOU 1829 CB SER A 237 24513 27724 17571 532 -1281 -2123 C ATOM 1830 OG SER A 237 -35.266 16.549 -29.247 1.00 0.00 O ATOM 1831 N ARG A 238 -36.494 16.974 -25.409 1.00163.65 N ANISOU 1831 N ARG A 238 21929 24553 15697 243 -1261 -2224 N ATOM 1832 CA ARG A 238 -36.060 16.550 -24.085 1.00157.15 C ANISOU 1832 CA ARG A 238 21206 23364 15138 198 -1146 -2273 C ATOM 1833 C ARG A 238 -37.262 15.872 -23.389 1.00163.95 C ANISOU 1833 C ARG A 238 22069 24085 16140 -59 -1247 -2456 C ATOM 1834 O ARG A 238 -38.294 16.536 -23.260 1.00163.43 O ANISOU 1834 O ARG A 238 21814 24183 16097 -177 -1391 -2407 O ATOM 1835 CB ARG A 238 -35.620 17.801 -23.285 1.00146.01 C ANISOU 1835 CB ARG A 238 19671 21848 13958 305 -1053 -1975 C ATOM 1836 CG ARG A 238 -34.464 18.603 -23.918 1.00137.88 C ANISOU 1836 CG ARG A 238 18616 20952 12818 526 -935 -1781 C ATOM 1837 CD ARG A 238 -34.903 19.687 -24.921 1.00134.29 C ANISOU 1837 CD ARG A 238 18001 20798 12226 570 -1020 -1575 C ATOM 1838 NE ARG A 238 -33.758 20.244 -25.652 1.00133.68 N ANISOU 1838 NE ARG A 238 17955 20901 11936 745 -914 -1471 N ATOM 1839 CZ ARG A 238 -33.829 21.169 -26.625 1.00135.70 C ANISOU 1839 CZ ARG A 238 18157 21443 11959 806 -973 -1355 C ATOM 1840 NH1 ARG A 238 -32.698 21.607 -27.193 1.00137.16 N1+ ANISOU 1840 NH1 ARG A 238 18386 21775 11953 953 -849 -1259 N1+ ATOM 1841 NH2 ARG A 238 -35.006 21.657 -27.044 1.00136.83 N1+ ANISOU 1841 NH2 ARG A 238 18200 21737 12053 726 -1155 -1332 N1+ ATOM 1842 N PRO A 239 -37.135 14.588 -22.966 1.00170.87 N ANISOU 1842 N PRO A 239 23159 24663 17102 -146 -1168 -2668 N ATOM 1843 CA PRO A 239 -38.177 13.875 -22.193 1.00169.65 C ANISOU 1843 CA PRO A 239 23020 24341 17098 -418 -1232 -2832 C ATOM 1844 C PRO A 239 -38.710 14.636 -20.967 1.00162.33 C ANISOU 1844 C PRO A 239 21894 23352 16432 -471 -1249 -2610 C ATOM 1845 O PRO A 239 -37.921 15.202 -20.209 1.00159.53 O ANISOU 1845 O PRO A 239 21519 22864 16229 -320 -1143 -2395 O ATOM 1846 CB PRO A 239 -37.492 12.564 -21.774 1.00171.61 C ANISOU 1846 CB PRO A 239 23576 24217 17413 -429 -1088 -3021 C ATOM 1847 CG PRO A 239 -36.473 12.310 -22.867 1.00173.38 C ANISOU 1847 CG PRO A 239 23941 24508 17429 -194 -1001 -3058 C ATOM 1848 CD PRO A 239 -35.987 13.712 -23.210 1.00171.71 C ANISOU 1848 CD PRO A 239 23509 24570 17162 5 -1007 -2768 C ATOM 1849 N LEU A 240 -40.044 14.633 -20.813 1.00153.73 N ANISOU 1849 N LEU A 240 20649 22376 15388 -691 -1383 -2677 N ATOM 1850 CA LEU A 240 -40.789 15.352 -19.772 1.00141.73 C ANISOU 1850 CA LEU A 240 18924 20829 14098 -748 -1406 -2487 C ATOM 1851 C LEU A 240 -40.498 14.883 -18.332 1.00130.52 C ANISOU 1851 C LEU A 240 17643 19021 12929 -796 -1263 -2464 C ATOM 1852 O LEU A 240 -40.845 15.607 -17.402 1.00129.73 O ANISOU 1852 O LEU A 240 17402 18862 13028 -825 -1254 -2299 O ATOM 1853 CB LEU A 240 -42.309 15.291 -20.072 1.00143.96 C ANISOU 1853 CB LEU A 240 19005 21324 14368 -978 -1572 -2601 C ATOM 1854 CG LEU A 240 -42.769 15.995 -21.372 1.00144.98 C ANISOU 1854 CG LEU A 240 18975 21877 14234 -940 -1749 -2636 C ATOM 1855 CD1 LEU A 240 -42.343 17.474 -21.439 1.00142.89 C ANISOU 1855 CD1 LEU A 240 18665 21780 13845 -639 -1731 -2372 C ATOM 1856 CD2 LEU A 240 -42.425 15.211 -22.655 1.00147.37 C ANISOU 1856 CD2 LEU A 240 19438 22240 14316 -1080 -1803 -2968 C ATOM 1857 N ARG A 241 -39.822 13.732 -18.166 1.00122.62 N ANISOU 1857 N ARG A 241 16925 17753 11911 -786 -1149 -2622 N ATOM 1858 CA ARG A 241 -39.280 13.255 -16.893 1.00114.72 C ANISOU 1858 CA ARG A 241 16081 16391 11117 -753 -1004 -2557 C ATOM 1859 C ARG A 241 -38.183 14.179 -16.323 1.00107.44 C ANISOU 1859 C ARG A 241 15047 15487 10287 -507 -942 -2263 C ATOM 1860 O ARG A 241 -38.044 14.227 -15.105 1.00105.34 O ANISOU 1860 O ARG A 241 14801 15008 10218 -494 -865 -2145 O ATOM 1861 CB ARG A 241 -38.756 11.810 -17.043 1.00114.81 C ANISOU 1861 CB ARG A 241 16430 16134 11058 -710 -891 -2757 C ATOM 1862 CG ARG A 241 -39.856 10.732 -17.150 1.00116.63 C ANISOU 1862 CG ARG A 241 16869 16080 11365 -980 -857 -2990 C ATOM 1863 CD ARG A 241 -40.466 10.505 -18.545 1.00120.19 C ANISOU 1863 CD ARG A 241 17323 16697 11648 -1217 -969 -3267 C ATOM 1864 NE ARG A 241 -39.511 9.868 -19.464 1.00125.01 N ANISOU 1864 NE ARG A 241 18139 17326 12033 -1097 -944 -3447 N ATOM 1865 CZ ARG A 241 -39.771 9.499 -20.730 1.00130.26 C ANISOU 1865 CZ ARG A 241 18946 17999 12550 -1297 -990 -3754 C ATOM 1866 NH1 ARG A 241 -38.806 8.923 -21.457 1.00133.20 N1+ ANISOU 1866 NH1 ARG A 241 19513 18385 12710 -1161 -957 -3910 N1+ ATOM 1867 NH2 ARG A 241 -40.980 9.690 -21.277 1.00131.86 N1+ ANISOU 1867 NH2 ARG A 241 19090 18199 12812 -1642 -1064 -3917 N1+ ATOM 1868 N VAL A 242 -37.459 14.915 -17.188 1.00103.81 N ANISOU 1868 N VAL A 242 14479 15285 9681 -324 -969 -2146 N ATOM 1869 CA VAL A 242 -36.490 15.942 -16.792 1.00100.06 C ANISOU 1869 CA VAL A 242 13882 14848 9286 -124 -907 -1875 C ATOM 1870 C VAL A 242 -37.197 17.212 -16.267 1.00 95.88 C ANISOU 1870 C VAL A 242 13118 14406 8906 -199 -978 -1691 C ATOM 1871 O VAL A 242 -36.736 17.787 -15.281 1.00 95.77 O ANISOU 1871 O VAL A 242 13049 14276 9064 -134 -913 -1514 O ATOM 1872 CB VAL A 242 -35.557 16.340 -17.976 1.00101.61 C ANISOU 1872 CB VAL A 242 14045 15290 9272 68 -896 -1809 C ATOM 1873 CG1 VAL A 242 -34.560 17.476 -17.653 1.00100.22 C ANISOU 1873 CG1 VAL A 242 13737 15157 9184 237 -823 -1535 C ATOM 1874 CG2 VAL A 242 -34.780 15.123 -18.512 1.00102.26 C ANISOU 1874 CG2 VAL A 242 14361 15287 9206 162 -811 -2001 C ATOM 1875 N LEU A 243 -38.311 17.600 -16.916 1.00 94.09 N ANISOU 1875 N LEU A 243 12747 14394 8609 -329 -1114 -1739 N ATOM 1876 CA LEU A 243 -39.137 18.758 -16.561 1.00 89.93 C ANISOU 1876 CA LEU A 243 11986 13981 8201 -360 -1184 -1562 C ATOM 1877 C LEU A 243 -39.881 18.585 -15.219 1.00 87.54 C ANISOU 1877 C LEU A 243 11677 13448 8135 -513 -1146 -1572 C ATOM 1878 O LEU A 243 -40.050 19.572 -14.503 1.00 84.60 O ANISOU 1878 O LEU A 243 11189 13036 7921 -466 -1118 -1382 O ATOM 1879 CB LEU A 243 -40.091 19.066 -17.744 1.00 90.47 C ANISOU 1879 CB LEU A 243 11896 14365 8115 -434 -1349 -1624 C ATOM 1880 CG LEU A 243 -40.965 20.335 -17.604 1.00 87.48 C ANISOU 1880 CG LEU A 243 11294 14207 7736 -316 -1420 -1382 C ATOM 1881 CD1 LEU A 243 -40.105 21.601 -17.438 1.00 86.71 C ANISOU 1881 CD1 LEU A 243 11239 14132 7576 -91 -1330 -1173 C ATOM 1882 CD2 LEU A 243 -41.931 20.468 -18.796 1.00 88.16 C ANISOU 1882 CD2 LEU A 243 11238 14627 7634 -358 -1596 -1460 C ATOM 1883 N THR A 244 -40.275 17.343 -14.888 1.00 88.45 N ANISOU 1883 N THR A 244 11930 13403 8274 -704 -1133 -1796 N ATOM 1884 CA THR A 244 -40.885 16.992 -13.604 1.00 87.42 C ANISOU 1884 CA THR A 244 11822 13043 8352 -866 -1077 -1810 C ATOM 1885 C THR A 244 -39.840 16.680 -12.509 1.00 85.79 C ANISOU 1885 C THR A 244 11790 12535 8270 -747 -932 -1713 C ATOM 1886 O THR A 244 -40.181 16.810 -11.335 1.00 86.30 O ANISOU 1886 O THR A 244 11853 12427 8508 -827 -877 -1654 O ATOM 1887 CB THR A 244 -41.836 15.772 -13.730 1.00 89.23 C ANISOU 1887 CB THR A 244 12160 13185 8559 -1136 -1096 -2084 C ATOM 1888 CG2 THR A 244 -43.004 16.000 -14.702 1.00 90.94 C ANISOU 1888 CG2 THR A 244 12169 13737 8649 -1267 -1258 -2198 C ATOM 1889 OG1 THR A 244 -41.152 14.583 -14.077 1.00 94.09 O ANISOU 1889 OG1 THR A 244 13059 13623 9067 -1100 -1025 -2244 O ATOM 1890 N ALA A 245 -38.598 16.308 -12.877 1.00 84.90 N ANISOU 1890 N ALA A 245 11818 12376 8063 -550 -869 -1698 N ATOM 1891 CA ALA A 245 -37.521 16.024 -11.923 1.00 84.22 C ANISOU 1891 CA ALA A 245 11891 12030 8077 -418 -744 -1623 C ATOM 1892 C ALA A 245 -36.973 17.276 -11.222 1.00 84.06 C ANISOU 1892 C ALA A 245 11706 12064 8169 -277 -721 -1372 C ATOM 1893 O ALA A 245 -36.655 17.196 -10.038 1.00 85.29 O ANISOU 1893 O ALA A 245 11915 12025 8467 -255 -652 -1294 O ATOM 1894 CB ALA A 245 -36.381 15.261 -12.613 1.00 84.39 C ANISOU 1894 CB ALA A 245 12109 11999 7956 -248 -680 -1717 C ATOM 1895 N VAL A 246 -36.886 18.402 -11.950 1.00 82.22 N ANISOU 1895 N VAL A 246 11289 12086 7864 -183 -776 -1246 N ATOM 1896 CA VAL A 246 -36.367 19.677 -11.442 1.00 79.66 C ANISOU 1896 CA VAL A 246 10828 11799 7641 -63 -743 -1019 C ATOM 1897 C VAL A 246 -37.313 20.413 -10.464 1.00 78.60 C ANISOU 1897 C VAL A 246 10578 11605 7682 -184 -765 -937 C ATOM 1898 O VAL A 246 -36.815 21.208 -9.667 1.00 75.88 O ANISOU 1898 O VAL A 246 10207 11157 7468 -127 -708 -805 O ATOM 1899 CB VAL A 246 -35.986 20.638 -12.600 1.00 78.71 C ANISOU 1899 CB VAL A 246 10571 11943 7394 50 -779 -901 C ATOM 1900 CG1 VAL A 246 -34.756 20.121 -13.368 1.00 79.98 C ANISOU 1900 CG1 VAL A 246 10838 12147 7402 203 -714 -945 C ATOM 1901 CG2 VAL A 246 -37.144 20.951 -13.565 1.00 80.12 C ANISOU 1901 CG2 VAL A 246 10647 12330 7467 -50 -902 -957 C ATOM 1902 N VAL A 247 -38.626 20.112 -10.498 1.00 80.39 N ANISOU 1902 N VAL A 247 10724 11911 7910 -352 -847 -1023 N ATOM 1903 CA VAL A 247 -39.589 20.569 -9.489 1.00 77.52 C ANISOU 1903 CA VAL A 247 10234 11512 7706 -465 -859 -958 C ATOM 1904 C VAL A 247 -39.699 19.576 -8.311 1.00 75.33 C ANISOU 1904 C VAL A 247 10107 10967 7546 -596 -782 -1048 C ATOM 1905 O VAL A 247 -39.868 20.023 -7.176 1.00 75.72 O ANISOU 1905 O VAL A 247 10097 10933 7740 -644 -747 -963 O ATOM 1906 CB VAL A 247 -41.018 20.812 -10.068 1.00 81.61 C ANISOU 1906 CB VAL A 247 10567 12262 8179 -580 -978 -1009 C ATOM 1907 CG1 VAL A 247 -41.040 21.949 -11.100 1.00 82.66 C ANISOU 1907 CG1 VAL A 247 10580 12657 8169 -430 -1056 -904 C ATOM 1908 CG2 VAL A 247 -41.721 19.577 -10.657 1.00 85.43 C ANISOU 1908 CG2 VAL A 247 11135 12735 8591 -774 -1016 -1252 C ATOM 1909 N ALA A 248 -39.591 18.263 -8.592 1.00 74.36 N ANISOU 1909 N ALA A 248 10198 10697 7357 -649 -744 -1216 N ATOM 1910 CA ALA A 248 -39.777 17.191 -7.615 1.00 74.09 C ANISOU 1910 CA ALA A 248 10356 10379 7417 -769 -656 -1294 C ATOM 1911 C ALA A 248 -38.587 17.022 -6.663 1.00 73.63 C ANISOU 1911 C ALA A 248 10452 10119 7406 -586 -560 -1191 C ATOM 1912 O ALA A 248 -38.811 16.928 -5.460 1.00 77.21 O ANISOU 1912 O ALA A 248 10973 10389 7974 -628 -494 -1137 O ATOM 1913 CB ALA A 248 -40.083 15.870 -8.335 1.00 76.95 C ANISOU 1913 CB ALA A 248 10908 10645 7687 -917 -651 -1529 C ATOM 1914 N SER A 249 -37.355 17.003 -7.202 1.00 71.63 N ANISOU 1914 N SER A 249 10247 9914 7055 -379 -550 -1163 N ATOM 1915 CA SER A 249 -36.122 16.857 -6.420 1.00 71.36 C ANISOU 1915 CA SER A 249 10324 9734 7055 -186 -472 -1072 C ATOM 1916 C SER A 249 -35.845 18.072 -5.523 1.00 70.37 C ANISOU 1916 C SER A 249 10031 9656 7050 -138 -470 -883 C ATOM 1917 O SER A 249 -35.348 17.892 -4.413 1.00 72.34 O ANISOU 1917 O SER A 249 10370 9740 7377 -85 -413 -823 O ATOM 1918 CB SER A 249 -34.923 16.608 -7.354 1.00 73.62 C ANISOU 1918 CB SER A 249 10645 10118 7209 22 -461 -1086 C ATOM 1919 OG SER A 249 -35.012 15.329 -7.946 1.00 78.40 O ANISOU 1919 OG SER A 249 11435 10657 7695 -7 -452 -1276 O ATOM 1920 N PHE A 250 -36.212 19.274 -6.002 1.00 67.06 N ANISOU 1920 N PHE A 250 9383 9458 6640 -151 -531 -789 N ATOM 1921 CA PHE A 250 -36.139 20.520 -5.243 1.00 63.48 C ANISOU 1921 CA PHE A 250 8782 9036 6300 -117 -524 -623 C ATOM 1922 C PHE A 250 -37.128 20.542 -4.061 1.00 62.95 C ANISOU 1922 C PHE A 250 8722 8838 6359 -268 -504 -621 C ATOM 1923 O PHE A 250 -36.749 20.974 -2.974 1.00 62.12 O ANISOU 1923 O PHE A 250 8627 8634 6342 -227 -459 -530 O ATOM 1924 CB PHE A 250 -36.324 21.712 -6.206 1.00 62.61 C ANISOU 1924 CB PHE A 250 8462 9163 6164 -96 -584 -525 C ATOM 1925 CG PHE A 250 -36.139 23.075 -5.566 1.00 61.56 C ANISOU 1925 CG PHE A 250 8198 9050 6142 -55 -567 -361 C ATOM 1926 CD1 PHE A 250 -34.838 23.547 -5.303 1.00 60.89 C ANISOU 1926 CD1 PHE A 250 8091 8988 6056 80 -524 -264 C ATOM 1927 CD2 PHE A 250 -37.244 23.795 -5.068 1.00 61.88 C ANISOU 1927 CD2 PHE A 250 8132 9094 6286 -157 -588 -316 C ATOM 1928 CE1 PHE A 250 -34.660 24.742 -4.622 1.00 60.44 C ANISOU 1928 CE1 PHE A 250 7928 8937 6099 95 -505 -132 C ATOM 1929 CE2 PHE A 250 -37.043 24.979 -4.371 1.00 61.78 C ANISOU 1929 CE2 PHE A 250 8021 9081 6371 -117 -564 -179 C ATOM 1930 CZ PHE A 250 -35.757 25.455 -4.155 1.00 60.73 C ANISOU 1930 CZ PHE A 250 7887 8952 6237 0 -524 -91 C ATOM 1931 N PHE A 251 -38.355 20.035 -4.279 1.00 63.36 N ANISOU 1931 N PHE A 251 8762 8901 6411 -450 -534 -730 N ATOM 1932 CA PHE A 251 -39.367 19.880 -3.236 1.00 61.97 C ANISOU 1932 CA PHE A 251 8569 8626 6350 -613 -501 -735 C ATOM 1933 C PHE A 251 -38.985 18.825 -2.183 1.00 64.31 C ANISOU 1933 C PHE A 251 9115 8646 6675 -642 -407 -780 C ATOM 1934 O PHE A 251 -38.934 19.159 -1.003 1.00 65.04 O ANISOU 1934 O PHE A 251 9231 8627 6853 -643 -351 -696 O ATOM 1935 CB PHE A 251 -40.756 19.637 -3.867 1.00 61.61 C ANISOU 1935 CB PHE A 251 8412 8705 6292 -811 -559 -853 C ATOM 1936 CG PHE A 251 -41.882 19.379 -2.877 1.00 62.62 C ANISOU 1936 CG PHE A 251 8513 8748 6531 -1004 -509 -882 C ATOM 1937 CD1 PHE A 251 -42.437 20.448 -2.141 1.00 62.23 C ANISOU 1937 CD1 PHE A 251 8270 8795 6581 -1004 -513 -771 C ATOM 1938 CD2 PHE A 251 -42.264 18.058 -2.557 1.00 63.45 C ANISOU 1938 CD2 PHE A 251 8799 8672 6639 -1190 -445 -1023 C ATOM 1939 CE1 PHE A 251 -43.386 20.198 -1.159 1.00 63.02 C ANISOU 1939 CE1 PHE A 251 8333 8835 6776 -1179 -453 -802 C ATOM 1940 CE2 PHE A 251 -43.212 17.829 -1.568 1.00 65.07 C ANISOU 1940 CE2 PHE A 251 8976 8806 6941 -1386 -379 -1048 C ATOM 1941 CZ PHE A 251 -43.774 18.895 -0.877 1.00 65.87 C ANISOU 1941 CZ PHE A 251 8862 9030 7137 -1378 -383 -938 C ATOM 1942 N ILE A 252 -38.719 17.584 -2.626 1.00 67.15 N ANISOU 1942 N ILE A 252 9683 8882 6951 -657 -384 -911 N ATOM 1943 CA ILE A 252 -38.456 16.419 -1.773 1.00 67.63 C ANISOU 1943 CA ILE A 252 10022 8650 7025 -676 -287 -951 C ATOM 1944 C ILE A 252 -37.194 16.537 -0.892 1.00 64.16 C ANISOU 1944 C ILE A 252 9657 8123 6597 -447 -249 -816 C ATOM 1945 O ILE A 252 -37.206 16.013 0.221 1.00 64.13 O ANISOU 1945 O ILE A 252 9806 7923 6637 -453 -177 -773 O ATOM 1946 CB ILE A 252 -38.414 15.103 -2.618 1.00 72.90 C ANISOU 1946 CB ILE A 252 10915 9194 7590 -711 -268 -1124 C ATOM 1947 CG1 ILE A 252 -39.806 14.749 -3.199 1.00 77.28 C ANISOU 1947 CG1 ILE A 252 11404 9820 8139 -990 -301 -1281 C ATOM 1948 CG2 ILE A 252 -37.785 13.862 -1.939 1.00 74.63 C ANISOU 1948 CG2 ILE A 252 11465 9083 7807 -668 -159 -1142 C ATOM 1949 CD1 ILE A 252 -40.869 14.322 -2.173 1.00 79.84 C ANISOU 1949 CD1 ILE A 252 11726 10036 8572 -1234 -239 -1293 C ATOM 1950 N CYS A 253 -36.155 17.239 -1.375 1.00 61.91 N ANISOU 1950 N CYS A 253 9258 7998 6266 -248 -295 -748 N ATOM 1951 CA CYS A 253 -34.943 17.510 -0.601 1.00 63.58 C ANISOU 1951 CA CYS A 253 9509 8167 6481 -35 -270 -639 C ATOM 1952 C CYS A 253 -35.190 18.560 0.495 1.00 66.08 C ANISOU 1952 C CYS A 253 9672 8537 6899 -57 -274 -507 C ATOM 1953 O CYS A 253 -34.898 18.284 1.659 1.00 70.36 O ANISOU 1953 O CYS A 253 10308 8965 7461 30 -237 -442 O ATOM 1954 CB CYS A 253 -33.758 17.939 -1.484 1.00 62.41 C ANISOU 1954 CB CYS A 253 9277 8186 6249 162 -303 -624 C ATOM 1955 SG CYS A 253 -33.090 16.516 -2.390 1.00 63.08 S ANISOU 1955 SG CYS A 253 9597 8170 6199 289 -272 -770 S ATOM 1956 N TRP A 254 -35.718 19.735 0.115 1.00 63.51 N ANISOU 1956 N TRP A 254 9122 8382 6627 -157 -319 -468 N ATOM 1957 CA TRP A 254 -35.829 20.883 1.017 1.00 58.82 C ANISOU 1957 CA TRP A 254 8378 7849 6121 -150 -321 -347 C ATOM 1958 C TRP A 254 -37.031 20.836 1.962 1.00 53.66 C ANISOU 1958 C TRP A 254 7713 7120 5556 -323 -286 -345 C ATOM 1959 O TRP A 254 -36.872 21.172 3.137 1.00 49.73 O ANISOU 1959 O TRP A 254 7195 6585 5117 -303 -257 -264 O ATOM 1960 CB TRP A 254 -35.793 22.207 0.231 1.00 59.38 C ANISOU 1960 CB TRP A 254 8222 8141 6197 -117 -377 -282 C ATOM 1961 CG TRP A 254 -34.427 22.543 -0.275 1.00 63.75 C ANISOU 1961 CG TRP A 254 8747 8786 6688 55 -387 -240 C ATOM 1962 CD1 TRP A 254 -33.945 22.297 -1.511 1.00 66.04 C ANISOU 1962 CD1 TRP A 254 9018 9192 6882 122 -409 -277 C ATOM 1963 CD2 TRP A 254 -33.301 23.045 0.504 1.00 63.42 C ANISOU 1963 CD2 TRP A 254 8682 8747 6668 175 -368 -163 C ATOM 1964 CE2 TRP A 254 -32.141 23.055 -0.328 1.00 62.73 C ANISOU 1964 CE2 TRP A 254 8543 8787 6504 302 -375 -157 C ATOM 1965 CE3 TRP A 254 -33.140 23.464 1.846 1.00 61.75 C ANISOU 1965 CE3 TRP A 254 8480 8460 6523 181 -347 -106 C ATOM 1966 NE1 TRP A 254 -32.600 22.599 -1.546 1.00 65.34 N ANISOU 1966 NE1 TRP A 254 8886 9180 6761 272 -394 -223 N ATOM 1967 CZ2 TRP A 254 -30.880 23.450 0.152 1.00 61.92 C ANISOU 1967 CZ2 TRP A 254 8379 8749 6400 423 -362 -103 C ATOM 1968 CZ3 TRP A 254 -31.881 23.858 2.341 1.00 60.07 C ANISOU 1968 CZ3 TRP A 254 8216 8307 6299 306 -348 -56 C ATOM 1969 CH2 TRP A 254 -30.753 23.844 1.498 1.00 61.00 C ANISOU 1969 CH2 TRP A 254 8263 8563 6351 420 -356 -57 C ATOM 1970 N PHE A 255 -38.210 20.440 1.463 1.00 54.83 N ANISOU 1970 N PHE A 255 7864 7259 5710 -498 -284 -441 N ATOM 1971 CA PHE A 255 -39.460 20.513 2.234 1.00 55.94 C ANISOU 1971 CA PHE A 255 7944 7373 5938 -672 -242 -443 C ATOM 1972 C PHE A 255 -39.495 19.797 3.608 1.00 57.17 C ANISOU 1972 C PHE A 255 8295 7309 6116 -701 -146 -419 C ATOM 1973 O PHE A 255 -40.028 20.400 4.536 1.00 54.87 O ANISOU 1973 O PHE A 255 7931 7024 5895 -739 -109 -353 O ATOM 1974 CB PHE A 255 -40.704 20.225 1.362 1.00 58.01 C ANISOU 1974 CB PHE A 255 8152 7696 6193 -869 -262 -570 C ATOM 1975 CG PHE A 255 -42.039 20.271 2.090 1.00 58.55 C ANISOU 1975 CG PHE A 255 8122 7774 6349 -1057 -213 -587 C ATOM 1976 CD1 PHE A 255 -42.594 21.512 2.468 1.00 57.90 C ANISOU 1976 CD1 PHE A 255 7806 7854 6339 -1034 -240 -506 C ATOM 1977 CD2 PHE A 255 -42.646 19.082 2.550 1.00 62.34 C ANISOU 1977 CD2 PHE A 255 8750 8097 6841 -1258 -128 -683 C ATOM 1978 CE1 PHE A 255 -43.750 21.554 3.235 1.00 60.89 C ANISOU 1978 CE1 PHE A 255 8076 8263 6797 -1190 -187 -527 C ATOM 1979 CE2 PHE A 255 -43.804 19.145 3.315 1.00 64.91 C ANISOU 1979 CE2 PHE A 255 8964 8453 7245 -1442 -67 -702 C ATOM 1980 CZ PHE A 255 -44.355 20.375 3.653 1.00 65.26 C ANISOU 1980 CZ PHE A 255 8751 8685 7359 -1400 -99 -627 C ATOM 1981 N PRO A 256 -38.902 18.590 3.763 1.00 55.12 N ANISOU 1981 N PRO A 256 8298 6850 5794 -676 -96 -467 N ATOM 1982 CA PRO A 256 -38.801 17.950 5.087 1.00 53.52 C ANISOU 1982 CA PRO A 256 8299 6438 5597 -684 -2 -419 C ATOM 1983 C PRO A 256 -38.051 18.794 6.131 1.00 53.45 C ANISOU 1983 C PRO A 256 8240 6470 5600 -517 -14 -292 C ATOM 1984 O PRO A 256 -38.562 18.979 7.233 1.00 53.51 O ANISOU 1984 O PRO A 256 8252 6431 5648 -583 44 -241 O ATOM 1985 CB PRO A 256 -38.114 16.605 4.793 1.00 46.88 C ANISOU 1985 CB PRO A 256 7756 5388 4668 -613 35 -478 C ATOM 1986 CG PRO A 256 -38.484 16.308 3.349 1.00 51.33 C ANISOU 1986 CG PRO A 256 8275 6022 5205 -702 -9 -606 C ATOM 1987 CD PRO A 256 -38.454 17.686 2.704 1.00 52.34 C ANISOU 1987 CD PRO A 256 8094 6436 5358 -650 -111 -571 C ATOM 1988 N PHE A 257 -36.886 19.332 5.745 1.00 54.51 N ANISOU 1988 N PHE A 257 8317 6702 5693 -314 -84 -250 N ATOM 1989 CA PHE A 257 -36.061 20.206 6.583 1.00 48.02 C ANISOU 1989 CA PHE A 257 7426 5941 4878 -177 -104 -151 C ATOM 1990 C PHE A 257 -36.798 21.502 6.944 1.00 46.12 C ANISOU 1990 C PHE A 257 6955 5839 4730 -268 -117 -108 C ATOM 1991 O PHE A 257 -36.874 21.879 8.113 1.00 45.45 O ANISOU 1991 O PHE A 257 6866 5732 4672 -268 -86 -53 O ATOM 1992 CB PHE A 257 -34.715 20.465 5.865 1.00 46.02 C ANISOU 1992 CB PHE A 257 7125 5793 4567 31 -170 -132 C ATOM 1993 CG PHE A 257 -33.742 21.453 6.494 1.00 44.35 C ANISOU 1993 CG PHE A 257 6775 5702 4376 129 -205 -52 C ATOM 1994 CD1 PHE A 257 -33.544 21.489 7.892 1.00 45.20 C ANISOU 1994 CD1 PHE A 257 6987 5735 4451 207 -188 -4 C ATOM 1995 CD2 PHE A 257 -32.897 22.223 5.666 1.00 41.01 C ANISOU 1995 CD2 PHE A 257 6126 5462 3992 134 -253 -27 C ATOM 1996 CE1 PHE A 257 -32.596 22.344 8.435 1.00 43.49 C ANISOU 1996 CE1 PHE A 257 6638 5640 4247 276 -226 47 C ATOM 1997 CE2 PHE A 257 -31.939 23.054 6.229 1.00 42.84 C ANISOU 1997 CE2 PHE A 257 6242 5789 4248 193 -276 30 C ATOM 1998 CZ PHE A 257 -31.798 23.123 7.607 1.00 43.86 C ANISOU 1998 CZ PHE A 257 6461 5857 4348 257 -267 57 C ATOM 1999 N GLN A 258 -37.385 22.115 5.916 1.00 49.09 N ANISOU 1999 N GLN A 258 7148 6359 5145 -332 -161 -134 N ATOM 2000 CA GLN A 258 -38.134 23.357 5.997 1.00 48.92 C ANISOU 2000 CA GLN A 258 6922 6456 5208 -392 -170 -90 C ATOM 2001 C GLN A 258 -39.381 23.283 6.894 1.00 51.05 C ANISOU 2001 C GLN A 258 7204 6658 5535 -547 -95 -108 C ATOM 2002 O GLN A 258 -39.613 24.186 7.693 1.00 48.22 O ANISOU 2002 O GLN A 258 6742 6342 5239 -559 -72 -60 O ATOM 2003 CB GLN A 258 -38.454 23.790 4.552 1.00 43.58 C ANISOU 2003 CB GLN A 258 6073 5945 4541 -408 -235 -106 C ATOM 2004 CG GLN A 258 -37.213 24.311 3.794 1.00 45.56 C ANISOU 2004 CG GLN A 258 6274 6294 4741 -262 -290 -67 C ATOM 2005 CD GLN A 258 -36.795 25.694 4.280 1.00 48.07 C ANISOU 2005 CD GLN A 258 6493 6664 5105 -186 -292 25 C ATOM 2006 NE2 GLN A 258 -35.821 26.326 3.640 1.00 45.77 N ANISOU 2006 NE2 GLN A 258 6170 6449 4771 -77 -320 57 N ATOM 2007 OE1 GLN A 258 -37.372 26.221 5.223 1.00 54.72 O ANISOU 2007 OE1 GLN A 258 7289 7482 6018 -233 -261 58 O ATOM 2008 N LEU A 259 -40.125 22.180 6.795 1.00 54.61 N ANISOU 2008 N LEU A 259 7784 6999 5964 -676 -45 -182 N ATOM 2009 CA LEU A 259 -41.300 21.874 7.610 1.00 56.21 C ANISOU 2009 CA LEU A 259 8006 7136 6215 -845 49 -203 C ATOM 2010 C LEU A 259 -40.938 21.680 9.093 1.00 60.25 C ANISOU 2010 C LEU A 259 8686 7505 6701 -794 124 -137 C ATOM 2011 O LEU A 259 -41.591 22.281 9.943 1.00 59.89 O ANISOU 2011 O LEU A 259 8577 7477 6701 -850 183 -106 O ATOM 2012 CB LEU A 259 -42.028 20.650 7.006 1.00 55.52 C ANISOU 2012 CB LEU A 259 8022 6964 6111 -1027 93 -311 C ATOM 2013 CG LEU A 259 -43.307 20.183 7.741 1.00 53.41 C ANISOU 2013 CG LEU A 259 7769 6634 5890 -1243 210 -346 C ATOM 2014 CD1 LEU A 259 -44.370 21.298 7.845 1.00 52.53 C ANISOU 2014 CD1 LEU A 259 7354 6740 5865 -1326 191 -364 C ATOM 2015 CD2 LEU A 259 -43.870 18.899 7.095 1.00 54.56 C ANISOU 2015 CD2 LEU A 259 8094 6633 6002 -1429 272 -454 C ATOM 2016 N VAL A 260 -39.872 20.915 9.367 1.00 61.12 N ANISOU 2016 N VAL A 260 9014 7483 6726 -672 121 -116 N ATOM 2017 CA VAL A 260 -39.320 20.723 10.710 1.00 57.72 C ANISOU 2017 CA VAL A 260 8753 6935 6242 -592 174 -46 C ATOM 2018 C VAL A 260 -38.799 22.048 11.311 1.00 57.63 C ANISOU 2018 C VAL A 260 8588 7056 6254 -480 124 17 C ATOM 2019 O VAL A 260 -39.094 22.348 12.469 1.00 62.21 O ANISOU 2019 O VAL A 260 9196 7609 6830 -498 180 55 O ATOM 2020 CB VAL A 260 -38.193 19.648 10.690 1.00 53.43 C ANISOU 2020 CB VAL A 260 8463 6246 5592 -440 163 -34 C ATOM 2021 CG1 VAL A 260 -37.354 19.529 11.979 1.00 52.39 C ANISOU 2021 CG1 VAL A 260 8487 6035 5383 -314 191 50 C ATOM 2022 CG2 VAL A 260 -38.778 18.265 10.350 1.00 54.89 C ANISOU 2022 CG2 VAL A 260 8852 6248 5755 -573 239 -102 C ATOM 2023 N ALA A 261 -38.095 22.850 10.499 1.00 54.93 N ANISOU 2023 N ALA A 261 8089 6853 5928 -373 27 23 N ATOM 2024 CA ALA A 261 -37.632 24.185 10.869 1.00 54.03 C ANISOU 2024 CA ALA A 261 7835 6851 5843 -295 -12 70 C ATOM 2025 C ALA A 261 -38.790 25.148 11.185 1.00 57.22 C ANISOU 2025 C ALA A 261 8083 7316 6342 -409 30 71 C ATOM 2026 O ALA A 261 -38.729 25.852 12.193 1.00 61.39 O ANISOU 2026 O ALA A 261 8575 7864 6886 -384 47 99 O ATOM 2027 CB ALA A 261 -36.731 24.752 9.765 1.00 50.18 C ANISOU 2027 CB ALA A 261 7222 6491 5355 -186 -103 76 C ATOM 2028 N LEU A 262 -39.844 25.135 10.358 1.00 56.89 N ANISOU 2028 N LEU A 262 7943 7314 6357 -527 45 30 N ATOM 2029 CA LEU A 262 -41.065 25.919 10.549 1.00 55.15 C ANISOU 2029 CA LEU A 262 7562 7168 6225 -610 86 28 C ATOM 2030 C LEU A 262 -41.790 25.555 11.861 1.00 55.32 C ANISOU 2030 C LEU A 262 7676 7099 6242 -709 201 20 C ATOM 2031 O LEU A 262 -42.158 26.454 12.617 1.00 57.80 O ANISOU 2031 O LEU A 262 7919 7445 6596 -706 246 39 O ATOM 2032 CB LEU A 262 -41.974 25.769 9.307 1.00 55.60 C ANISOU 2032 CB LEU A 262 7468 7329 6328 -693 56 -18 C ATOM 2033 CG LEU A 262 -43.235 26.662 9.290 1.00 57.22 C ANISOU 2033 CG LEU A 262 7485 7637 6620 -757 94 -26 C ATOM 2034 CD1 LEU A 262 -42.878 28.166 9.286 1.00 56.56 C ANISOU 2034 CD1 LEU A 262 7312 7597 6580 -634 77 39 C ATOM 2035 CD2 LEU A 262 -44.160 26.275 8.116 1.00 60.38 C ANISOU 2035 CD2 LEU A 262 7723 8174 7044 -818 39 -75 C ATOM 2036 N LEU A 263 -41.908 24.250 12.147 1.00 55.60 N ANISOU 2036 N LEU A 263 7886 7013 6227 -800 261 -8 N ATOM 2037 CA LEU A 263 -42.423 23.733 13.418 1.00 54.38 C ANISOU 2037 CA LEU A 263 7843 6764 6054 -909 391 -6 C ATOM 2038 C LEU A 263 -41.564 24.181 14.617 1.00 56.80 C ANISOU 2038 C LEU A 263 8266 7019 6296 -792 409 57 C ATOM 2039 O LEU A 263 -42.107 24.642 15.618 1.00 56.97 O ANISOU 2039 O LEU A 263 8282 7042 6323 -843 500 65 O ATOM 2040 CB LEU A 263 -42.533 22.197 13.359 1.00 53.27 C ANISOU 2040 CB LEU A 263 7913 6467 5861 -1028 460 -38 C ATOM 2041 CG LEU A 263 -43.683 21.667 12.476 1.00 54.49 C ANISOU 2041 CG LEU A 263 7959 6671 6074 -1210 470 -129 C ATOM 2042 CD1 LEU A 263 -43.510 20.158 12.197 1.00 57.84 C ANISOU 2042 CD1 LEU A 263 8640 6899 6438 -1329 544 -168 C ATOM 2043 CD2 LEU A 263 -45.068 22.007 13.072 1.00 51.14 C ANISOU 2043 CD2 LEU A 263 7323 6373 5735 -1358 547 -165 C ATOM 2044 N GLY A 264 -40.234 24.125 14.475 1.00 57.60 N ANISOU 2044 N GLY A 264 8463 7097 6326 -632 322 91 N ATOM 2045 CA GLY A 264 -39.295 24.620 15.482 1.00 57.39 C ANISOU 2045 CA GLY A 264 8517 7062 6226 -517 313 136 C ATOM 2046 C GLY A 264 -39.471 26.130 15.734 1.00 59.46 C ANISOU 2046 C GLY A 264 8591 7443 6556 -496 293 130 C ATOM 2047 O GLY A 264 -39.411 26.562 16.881 1.00 64.48 O ANISOU 2047 O GLY A 264 9278 8073 7148 -474 332 141 O ATOM 2048 N THR A 265 -39.747 26.915 14.684 1.00 57.08 N ANISOU 2048 N THR A 265 8091 7244 6355 -500 237 112 N ATOM 2049 CA THR A 265 -39.902 28.373 14.727 1.00 56.95 C ANISOU 2049 CA THR A 265 7920 7309 6409 -475 229 111 C ATOM 2050 C THR A 265 -41.116 28.849 15.566 1.00 57.90 C ANISOU 2050 C THR A 265 7990 7431 6581 -566 343 90 C ATOM 2051 O THR A 265 -40.997 29.820 16.310 1.00 57.99 O ANISOU 2051 O THR A 265 7983 7450 6598 -537 378 84 O ATOM 2052 CB THR A 265 -40.012 28.962 13.290 1.00 55.64 C ANISOU 2052 CB THR A 265 7583 7234 6323 -445 152 115 C ATOM 2053 CG2 THR A 265 -40.008 30.495 13.198 1.00 54.71 C ANISOU 2053 CG2 THR A 265 7343 7165 6279 -410 155 123 C ATOM 2054 OG1 THR A 265 -38.909 28.534 12.509 1.00 54.52 O ANISOU 2054 OG1 THR A 265 7481 7107 6127 -361 62 130 O ATOM 2055 N VAL A 266 -42.247 28.138 15.484 1.00 56.19 N ANISOU 2055 N VAL A 266 7741 7213 6397 -682 406 67 N ATOM 2056 CA VAL A 266 -43.449 28.412 16.279 1.00 56.75 C ANISOU 2056 CA VAL A 266 7737 7312 6514 -773 526 40 C ATOM 2057 C VAL A 266 -43.382 27.820 17.707 1.00 58.63 C ANISOU 2057 C VAL A 266 8166 7454 6657 -820 639 49 C ATOM 2058 O VAL A 266 -44.144 28.268 18.564 1.00 63.37 O ANISOU 2058 O VAL A 266 8722 8081 7276 -871 751 29 O ATOM 2059 CB VAL A 266 -44.736 27.893 15.578 1.00 56.29 C ANISOU 2059 CB VAL A 266 7546 7321 6521 -901 556 -2 C ATOM 2060 CG1 VAL A 266 -44.984 28.628 14.249 1.00 54.60 C ANISOU 2060 CG1 VAL A 266 7197 7194 6356 -846 428 -2 C ATOM 2061 CG2 VAL A 266 -44.792 26.368 15.370 1.00 56.67 C ANISOU 2061 CG2 VAL A 266 7765 7263 6505 -1042 630 -18 C ATOM 2062 N TRP A 267 -42.448 26.885 17.942 1.00 58.96 N ANISOU 2062 N TRP A 267 8423 7390 6588 -788 615 83 N ATOM 2063 CA TRP A 267 -42.219 26.201 19.216 1.00 60.50 C ANISOU 2063 CA TRP A 267 8837 7486 6664 -808 713 111 C ATOM 2064 C TRP A 267 -40.963 26.699 19.957 1.00 63.23 C ANISOU 2064 C TRP A 267 9290 7828 6908 -652 638 141 C ATOM 2065 O TRP A 267 -40.529 26.037 20.900 1.00 66.27 O ANISOU 2065 O TRP A 267 9895 8131 7155 -611 665 182 O ATOM 2066 CB TRP A 267 -42.171 24.672 18.986 1.00 60.44 C ANISOU 2066 CB TRP A 267 9029 7344 6590 -888 761 133 C ATOM 2067 CG TRP A 267 -43.432 24.001 18.522 1.00 62.80 C ANISOU 2067 CG TRP A 267 9251 7643 6968 -1091 868 88 C ATOM 2068 CD1 TRP A 267 -44.697 24.417 18.765 1.00 62.00 C ANISOU 2068 CD1 TRP A 267 8968 7642 6948 -1206 968 44 C ATOM 2069 CD2 TRP A 267 -43.564 22.715 17.843 1.00 65.25 C ANISOU 2069 CD2 TRP A 267 9651 7859 7280 -1207 885 66 C ATOM 2070 CE2 TRP A 267 -44.953 22.430 17.675 1.00 63.94 C ANISOU 2070 CE2 TRP A 267 9338 7758 7200 -1415 993 3 C ATOM 2071 CE3 TRP A 267 -42.651 21.750 17.360 1.00 66.16 C ANISOU 2071 CE3 TRP A 267 9959 7847 7333 -1153 823 84 C ATOM 2072 NE1 TRP A 267 -45.594 23.504 18.251 1.00 62.43 N ANISOU 2072 NE1 TRP A 267 8971 7695 7055 -1399 1041 -5 N ATOM 2073 CZ2 TRP A 267 -45.410 21.257 17.049 1.00 65.71 C ANISOU 2073 CZ2 TRP A 267 9599 7920 7447 -1598 1036 -51 C ATOM 2074 CZ3 TRP A 267 -43.096 20.558 16.751 1.00 68.13 C ANISOU 2074 CZ3 TRP A 267 10273 8010 7606 -1318 874 34 C ATOM 2075 CH2 TRP A 267 -44.473 20.316 16.586 1.00 67.72 C ANISOU 2075 CH2 TRP A 267 10070 8022 7638 -1553 978 -37 C ATOM 2076 N LEU A 268 -40.399 27.859 19.585 1.00 61.57 N ANISOU 2076 N LEU A 268 8928 7710 6755 -566 544 118 N ATOM 2077 CA LEU A 268 -39.204 28.416 20.241 1.00 59.36 C ANISOU 2077 CA LEU A 268 8714 7455 6385 -443 462 122 C ATOM 2078 C LEU A 268 -39.391 28.652 21.751 1.00 60.63 C ANISOU 2078 C LEU A 268 8994 7600 6443 -448 551 115 C ATOM 2079 O LEU A 268 -38.515 28.290 22.535 1.00 62.15 O ANISOU 2079 O LEU A 268 9358 7771 6485 -369 520 142 O ATOM 2080 CB LEU A 268 -38.744 29.713 19.543 1.00 56.10 C ANISOU 2080 CB LEU A 268 8115 7132 6070 -396 373 90 C ATOM 2081 CG LEU A 268 -38.134 29.503 18.145 1.00 54.96 C ANISOU 2081 CG LEU A 268 7898 7026 5960 -338 251 105 C ATOM 2082 CD1 LEU A 268 -37.947 30.847 17.428 1.00 52.82 C ANISOU 2082 CD1 LEU A 268 7449 6823 5797 -328 206 84 C ATOM 2083 CD2 LEU A 268 -36.820 28.696 18.186 1.00 54.31 C ANISOU 2083 CD2 LEU A 268 7937 6952 5746 -229 164 121 C ATOM 2084 N LYS A 269 -40.555 29.187 22.146 1.00 62.36 N ANISOU 2084 N LYS A 269 9122 7841 6731 -524 660 78 N ATOM 2085 CA LYS A 269 -40.908 29.394 23.552 1.00 65.71 C ANISOU 2085 CA LYS A 269 9657 8260 7052 -530 760 61 C ATOM 2086 C LYS A 269 -41.168 28.076 24.304 1.00 66.55 C ANISOU 2086 C LYS A 269 9981 8280 7024 -580 864 118 C ATOM 2087 O LYS A 269 -40.906 28.011 25.503 1.00 64.91 O ANISOU 2087 O LYS A 269 9943 8061 6661 -539 902 132 O ATOM 2088 CB LYS A 269 -42.124 30.334 23.647 1.00 69.23 C ANISOU 2088 CB LYS A 269 9948 8750 7606 -586 870 4 C ATOM 2089 CG LYS A 269 -41.822 31.760 23.155 1.00 69.10 C ANISOU 2089 CG LYS A 269 9774 8784 7698 -521 789 -46 C ATOM 2090 CD LYS A 269 -43.026 32.700 23.306 1.00 70.45 C ANISOU 2090 CD LYS A 269 9830 8982 7955 -538 910 -101 C ATOM 2091 CE LYS A 269 -42.733 34.117 22.796 1.00 72.85 C ANISOU 2091 CE LYS A 269 10039 9293 8348 -463 844 -148 C ATOM 2092 NZ LYS A 269 -43.909 34.992 22.945 1.00 75.54 N1+ ANISOU 2092 NZ LYS A 269 10295 9643 8763 -444 966 -205 N1+ ATOM 2093 N GLU A 270 -41.640 27.045 23.584 1.00 69.43 N ANISOU 2093 N GLU A 270 10361 8581 7439 -675 914 150 N ATOM 2094 CA GLU A 270 -41.869 25.699 24.106 1.00 69.93 C ANISOU 2094 CA GLU A 270 10668 8526 7377 -734 1020 213 C ATOM 2095 C GLU A 270 -40.550 24.976 24.432 1.00 70.09 C ANISOU 2095 C GLU A 270 10910 8482 7239 -582 913 278 C ATOM 2096 O GLU A 270 -40.451 24.371 25.498 1.00 70.37 O ANISOU 2096 O GLU A 270 11192 8435 7109 -560 987 341 O ATOM 2097 CB GLU A 270 -42.726 24.900 23.102 1.00 72.51 C ANISOU 2097 CB GLU A 270 10956 8790 7803 -891 1092 212 C ATOM 2098 CG GLU A 270 -44.095 25.525 22.764 1.00 76.64 C ANISOU 2098 CG GLU A 270 11238 9410 8473 -1035 1195 146 C ATOM 2099 CD GLU A 270 -45.046 25.518 23.960 1.00 84.79 C ANISOU 2099 CD GLU A 270 12333 10442 9441 -1136 1392 145 C ATOM 2100 OE1 GLU A 270 -45.737 24.490 24.128 1.00 89.10 O ANISOU 2100 OE1 GLU A 270 13054 10883 9917 -1268 1526 184 O ATOM 2101 OE2 GLU A 270 -45.053 26.531 24.693 1.00 86.80 O1- ANISOU 2101 OE2 GLU A 270 12477 10793 9709 -1086 1423 104 O1- ATOM 2102 N MET A 271 -39.562 25.123 23.542 1.00 71.56 N ANISOU 2102 N MET A 271 11010 8715 7464 -466 743 267 N ATOM 2103 CA MET A 271 -38.196 24.655 23.753 1.00 72.90 C ANISOU 2103 CA MET A 271 11349 8863 7487 -293 628 318 C ATOM 2104 C MET A 271 -37.473 25.456 24.856 1.00 72.77 C ANISOU 2104 C MET A 271 11346 8956 7348 -173 553 299 C ATOM 2105 O MET A 271 -36.734 24.856 25.630 1.00 75.64 O ANISOU 2105 O MET A 271 11896 9310 7532 -33 498 352 O ATOM 2106 CB MET A 271 -37.421 24.661 22.418 1.00 71.53 C ANISOU 2106 CB MET A 271 11060 8721 7397 -218 488 305 C ATOM 2107 CG MET A 271 -37.903 23.569 21.444 1.00 73.44 C ANISOU 2107 CG MET A 271 11309 8859 7735 -326 541 309 C ATOM 2108 SD MET A 271 -36.995 23.456 19.877 1.00 72.88 S ANISOU 2108 SD MET A 271 11127 8833 7732 -221 385 290 S ATOM 2109 CE MET A 271 -37.665 24.889 18.999 1.00 70.76 C ANISOU 2109 CE MET A 271 10533 8748 7602 -237 304 225 C ATOM 2110 N LEU A 272 -37.723 26.770 24.944 1.00 69.95 N ANISOU 2110 N LEU A 272 10800 8702 7075 -219 548 221 N ATOM 2111 CA LEU A 272 -37.137 27.662 25.950 1.00 68.71 C ANISOU 2111 CA LEU A 272 10642 8654 6810 -129 469 174 C ATOM 2112 C LEU A 272 -37.596 27.342 27.389 1.00 69.51 C ANISOU 2112 C LEU A 272 10932 8735 6744 -139 583 190 C ATOM 2113 O LEU A 272 -36.780 26.940 28.216 1.00 70.98 O ANISOU 2113 O LEU A 272 11250 8979 6739 -20 510 200 O ATOM 2114 CB LEU A 272 -37.422 29.133 25.549 1.00 67.46 C ANISOU 2114 CB LEU A 272 10247 8582 6805 -181 434 78 C ATOM 2115 CG LEU A 272 -36.856 30.231 26.481 1.00 69.57 C ANISOU 2115 CG LEU A 272 10499 8950 6984 -138 374 -4 C ATOM 2116 CD1 LEU A 272 -35.318 30.185 26.574 1.00 69.11 C ANISOU 2116 CD1 LEU A 272 10470 8992 6798 -6 201 -4 C ATOM 2117 CD2 LEU A 272 -37.371 31.624 26.070 1.00 68.58 C ANISOU 2117 CD2 LEU A 272 10175 8853 7031 -209 378 -92 C ATOM 2118 N PHE A 273 -38.883 27.571 27.676 1.00 66.88 N ANISOU 2118 N PHE A 273 10604 8339 6467 -276 761 190 N ATOM 2119 CA PHE A 273 -39.445 27.560 29.028 1.00 62.72 C ANISOU 2119 CA PHE A 273 10235 7806 5791 -304 898 196 C ATOM 2120 C PHE A 273 -39.728 26.163 29.603 1.00 63.53 C ANISOU 2120 C PHE A 273 10612 7785 5742 -316 1010 312 C ATOM 2121 O PHE A 273 -39.783 26.042 30.827 1.00 68.06 O ANISOU 2121 O PHE A 273 11369 8357 6135 -304 1106 340 O ATOM 2122 CB PHE A 273 -40.720 28.430 29.070 1.00 61.18 C ANISOU 2122 CB PHE A 273 9883 7629 5732 -440 1052 126 C ATOM 2123 CG PHE A 273 -40.484 29.919 28.872 1.00 60.67 C ANISOU 2123 CG PHE A 273 9642 7662 5747 -408 985 13 C ATOM 2124 CD1 PHE A 273 -39.785 30.663 29.847 1.00 61.42 C ANISOU 2124 CD1 PHE A 273 9821 7819 5697 -360 992 -50 C ATOM 2125 CD2 PHE A 273 -40.897 30.564 27.686 1.00 61.14 C ANISOU 2125 CD2 PHE A 273 9472 7741 6017 -428 920 -32 C ATOM 2126 CE1 PHE A 273 -39.537 32.015 29.644 1.00 61.68 C ANISOU 2126 CE1 PHE A 273 9718 7913 5805 -346 942 -167 C ATOM 2127 CE2 PHE A 273 -40.642 31.916 27.504 1.00 60.74 C ANISOU 2127 CE2 PHE A 273 9294 7745 6040 -404 874 -129 C ATOM 2128 CZ PHE A 273 -39.968 32.639 28.480 1.00 61.58 C ANISOU 2128 CZ PHE A 273 9493 7894 6012 -370 889 -202 C ATOM 2129 N TYR A 274 -39.924 25.152 28.738 1.00 62.35 N ANISOU 2129 N TYR A 274 10516 7522 5652 -343 1010 379 N ATOM 2130 CA TYR A 274 -40.354 23.808 29.146 1.00 63.08 C ANISOU 2130 CA TYR A 274 10898 7456 5612 -375 1140 490 C ATOM 2131 C TYR A 274 -39.453 22.689 28.602 1.00 65.71 C ANISOU 2131 C TYR A 274 11391 7679 5897 -255 1039 571 C ATOM 2132 O TYR A 274 -39.525 21.576 29.124 1.00 67.82 O ANISOU 2132 O TYR A 274 11953 7790 6024 -245 1136 676 O ATOM 2133 CB TYR A 274 -41.810 23.576 28.687 1.00 64.03 C ANISOU 2133 CB TYR A 274 10971 7496 5864 -614 1348 482 C ATOM 2134 CG TYR A 274 -42.807 24.635 29.123 1.00 66.09 C ANISOU 2134 CG TYR A 274 11042 7871 6198 -724 1464 396 C ATOM 2135 CD1 TYR A 274 -43.165 24.752 30.482 1.00 69.87 C ANISOU 2135 CD1 TYR A 274 11669 8355 6522 -761 1626 417 C ATOM 2136 CD2 TYR A 274 -43.369 25.515 28.174 1.00 65.78 C ANISOU 2136 CD2 TYR A 274 10686 7935 6374 -773 1418 298 C ATOM 2137 CE1 TYR A 274 -44.073 25.748 30.890 1.00 70.71 C ANISOU 2137 CE1 TYR A 274 11602 8571 6694 -843 1742 330 C ATOM 2138 CE2 TYR A 274 -44.277 26.510 28.581 1.00 66.61 C ANISOU 2138 CE2 TYR A 274 10626 8138 6546 -841 1527 220 C ATOM 2139 CZ TYR A 274 -44.628 26.629 29.940 1.00 69.36 C ANISOU 2139 CZ TYR A 274 11115 8493 6746 -875 1690 230 C ATOM 2140 OH TYR A 274 -45.507 27.596 30.334 1.00 70.44 O ANISOU 2140 OH TYR A 274 11086 8730 6947 -925 1808 144 O ATOM 2141 N GLY A 275 -38.649 22.969 27.559 1.00 66.70 N ANISOU 2141 N GLY A 275 11349 7868 6124 -161 863 529 N ATOM 2142 CA GLY A 275 -37.839 21.966 26.861 1.00 67.13 C ANISOU 2142 CA GLY A 275 11548 7817 6143 -43 786 594 C ATOM 2143 C GLY A 275 -38.684 21.030 25.974 1.00 70.09 C ANISOU 2143 C GLY A 275 11998 8009 6626 -210 915 616 C ATOM 2144 O GLY A 275 -38.171 19.998 25.543 1.00 72.69 O ANISOU 2144 O GLY A 275 12563 8177 6879 -134 920 690 O ATOM 2145 N LYS A 276 -39.961 21.366 25.718 1.00 69.97 N ANISOU 2145 N LYS A 276 11789 8017 6780 -432 1020 547 N ATOM 2146 CA LYS A 276 -40.907 20.617 24.887 1.00 72.68 C ANISOU 2146 CA LYS A 276 12164 8221 7231 -627 1140 540 C ATOM 2147 C LYS A 276 -40.502 20.595 23.405 1.00 69.62 C ANISOU 2147 C LYS A 276 11628 7849 6977 -594 1006 488 C ATOM 2148 O LYS A 276 -39.900 21.552 22.923 1.00 67.25 O ANISOU 2148 O LYS A 276 11160 7682 6708 -444 837 456 O ATOM 2149 CB LYS A 276 -42.306 21.246 25.039 1.00 73.84 C ANISOU 2149 CB LYS A 276 12124 8433 7499 -865 1294 476 C ATOM 2150 CG LYS A 276 -42.994 20.938 26.379 1.00 77.75 C ANISOU 2150 CG LYS A 276 12766 8913 7863 -923 1462 520 C ATOM 2151 CD LYS A 276 -44.255 21.790 26.629 1.00 80.23 C ANISOU 2151 CD LYS A 276 12827 9350 8307 -1110 1590 436 C ATOM 2152 CE LYS A 276 -45.370 21.647 25.579 1.00 83.20 C ANISOU 2152 CE LYS A 276 13174 9647 8790 -1369 1747 412 C ATOM 2153 NZ LYS A 276 -45.894 20.273 25.505 1.00 86.90 N1+ ANISOU 2153 NZ LYS A 276 13967 9938 9114 -1490 1952 499 N1+ ATOM 2154 N TYR A 277 -40.897 19.513 22.715 1.00 68.88 N ANISOU 2154 N TYR A 277 11602 7616 6952 -752 1092 475 N ATOM 2155 CA TYR A 277 -40.676 19.252 21.288 1.00 70.55 C ANISOU 2155 CA TYR A 277 11687 7835 7282 -756 990 413 C ATOM 2156 C TYR A 277 -39.195 18.995 20.950 1.00 70.60 C ANISOU 2156 C TYR A 277 11791 7828 7204 -490 829 450 C ATOM 2157 O TYR A 277 -38.674 19.558 19.987 1.00 70.80 O ANISOU 2157 O TYR A 277 11607 7988 7308 -401 686 400 O ATOM 2158 CB TYR A 277 -41.335 20.329 20.387 1.00 69.78 C ANISOU 2158 CB TYR A 277 11211 7945 7357 -834 926 320 C ATOM 2159 CG TYR A 277 -42.816 20.543 20.647 1.00 69.52 C ANISOU 2159 CG TYR A 277 11038 7961 7417 -1072 1075 272 C ATOM 2160 CD1 TYR A 277 -43.763 19.610 20.178 1.00 69.38 C ANISOU 2160 CD1 TYR A 277 11019 7871 7473 -1296 1177 223 C ATOM 2161 CD2 TYR A 277 -43.249 21.677 21.363 1.00 68.24 C ANISOU 2161 CD2 TYR A 277 10734 7929 7266 -1072 1115 262 C ATOM 2162 CE1 TYR A 277 -45.136 19.813 20.421 1.00 68.80 C ANISOU 2162 CE1 TYR A 277 10780 7879 7483 -1512 1312 169 C ATOM 2163 CE2 TYR A 277 -44.620 21.878 21.610 1.00 67.54 C ANISOU 2163 CE2 TYR A 277 10497 7906 7260 -1265 1257 214 C ATOM 2164 CZ TYR A 277 -45.565 20.948 21.137 1.00 67.74 C ANISOU 2164 CZ TYR A 277 10496 7883 7359 -1484 1353 169 C ATOM 2165 OH TYR A 277 -46.893 21.148 21.373 1.00 68.00 O ANISOU 2165 OH TYR A 277 10347 8017 7473 -1675 1492 112 O ATOM 2166 N LYS A 278 -38.526 18.108 21.704 1.00 69.15 N ANISOU 2166 N LYS A 278 11934 7489 6853 -354 859 544 N ATOM 2167 CA LYS A 278 -37.181 17.629 21.344 1.00 70.28 C ANISOU 2167 CA LYS A 278 12181 7616 6905 -83 717 579 C ATOM 2168 C LYS A 278 -37.156 16.677 20.132 1.00 74.28 C ANISOU 2168 C LYS A 278 12728 8008 7488 -103 701 533 C ATOM 2169 O LYS A 278 -36.082 16.422 19.586 1.00 76.76 O ANISOU 2169 O LYS A 278 13052 8352 7761 119 575 535 O ATOM 2170 CB LYS A 278 -36.454 17.042 22.574 1.00 71.37 C ANISOU 2170 CB LYS A 278 12674 7614 6828 96 755 702 C ATOM 2171 CG LYS A 278 -35.862 18.096 23.535 1.00 73.26 C ANISOU 2171 CG LYS A 278 12889 7993 6951 166 739 743 C ATOM 2172 CD LYS A 278 -34.946 19.113 22.827 1.00 76.36 C ANISOU 2172 CD LYS A 278 13634 8276 7105 393 743 871 C ATOM 2173 CE LYS A 278 -33.983 19.881 23.735 1.00 78.71 C ANISOU 2173 CE LYS A 278 13927 8713 7264 439 739 903 C ATOM 2174 NZ LYS A 278 -33.219 20.863 22.946 1.00 81.72 N1+ ANISOU 2174 NZ LYS A 278 14310 9044 7694 160 936 892 N1+ ATOM 2175 N ILE A 279 -38.335 16.229 19.677 1.00 73.85 N ANISOU 2175 N ILE A 279 12687 7838 7535 -366 827 479 N ATOM 2176 CA ILE A 279 -38.526 15.533 18.406 1.00 68.51 C ANISOU 2176 CA ILE A 279 12033 7068 6931 -416 810 408 C ATOM 2177 C ILE A 279 -38.076 16.352 17.176 1.00 67.54 C ANISOU 2177 C ILE A 279 11573 7174 6914 -350 649 327 C ATOM 2178 O ILE A 279 -37.570 15.755 16.229 1.00 67.43 O ANISOU 2178 O ILE A 279 11581 7126 6915 -277 587 281 O ATOM 2179 CB ILE A 279 -40.014 15.103 18.231 1.00 64.96 C ANISOU 2179 CB ILE A 279 11632 6484 6568 -751 977 347 C ATOM 2180 CG1 ILE A 279 -40.231 14.174 17.014 1.00 67.24 C ANISOU 2180 CG1 ILE A 279 12041 6616 6889 -802 977 272 C ATOM 2181 CG2 ILE A 279 -41.010 16.287 18.195 1.00 57.91 C ANISOU 2181 CG2 ILE A 279 10367 5816 5818 -951 977 268 C ATOM 2182 CD1 ILE A 279 -41.548 13.387 17.056 1.00 70.57 C ANISOU 2182 CD1 ILE A 279 12536 6895 7383 -1152 1142 196 C ATOM 2183 N ILE A 280 -38.083 17.694 17.273 1.00 65.60 N ANISOU 2183 N ILE A 280 11035 7155 6737 -371 590 311 N ATOM 2184 CA ILE A 280 -37.460 18.600 16.303 1.00 65.53 C ANISOU 2184 CA ILE A 280 10729 7351 6817 -305 450 253 C ATOM 2185 C ILE A 280 -35.947 18.338 16.129 1.00 71.60 C ANISOU 2185 C ILE A 280 11530 8178 7496 -24 320 286 C ATOM 2186 O ILE A 280 -35.499 18.171 14.996 1.00 77.98 O ANISOU 2186 O ILE A 280 12243 9049 8335 55 235 243 O ATOM 2187 CB ILE A 280 -37.686 20.097 16.685 1.00 63.36 C ANISOU 2187 CB ILE A 280 10172 7268 6633 -390 436 234 C ATOM 2188 CG1 ILE A 280 -39.186 20.468 16.677 1.00 61.66 C ANISOU 2188 CG1 ILE A 280 9889 7031 6510 -652 564 191 C ATOM 2189 CG2 ILE A 280 -36.875 21.132 15.866 1.00 62.44 C ANISOU 2189 CG2 ILE A 280 9784 7342 6599 -318 303 192 C ATOM 2190 CD1 ILE A 280 -39.866 20.376 15.301 1.00 60.01 C ANISOU 2190 CD1 ILE A 280 9608 6806 6386 -794 565 110 C ATOM 2191 N ASP A 281 -35.200 18.246 17.240 1.00 73.07 N ANISOU 2191 N ASP A 281 11846 8361 7558 135 303 360 N ATOM 2192 CA ASP A 281 -33.751 18.001 17.257 1.00 75.70 C ANISOU 2192 CA ASP A 281 12190 8779 7793 413 175 387 C ATOM 2193 C ASP A 281 -33.386 16.638 16.639 1.00 72.31 C ANISOU 2193 C ASP A 281 11999 8179 7295 551 182 399 C ATOM 2194 O ASP A 281 -32.382 16.527 15.939 1.00 72.43 O ANISOU 2194 O ASP A 281 11938 8291 7292 739 79 376 O ATOM 2195 CB ASP A 281 -33.068 18.125 18.645 1.00 82.75 C ANISOU 2195 CB ASP A 281 13176 9719 8546 552 150 457 C ATOM 2196 CG ASP A 281 -33.414 19.350 19.503 1.00 87.09 C ANISOU 2196 CG ASP A 281 13526 10413 9151 418 157 433 C ATOM 2197 OD1 ASP A 281 -34.603 19.729 19.557 1.00 88.28 O ANISOU 2197 OD1 ASP A 281 13517 10580 9444 208 215 382 O ATOM 2198 OD2 ASP A 281 -32.498 19.809 20.222 1.00 88.56 O1- ANISOU 2198 OD2 ASP A 281 13715 10702 9231 533 101 460 O1- ATOM 2199 N ILE A 282 -34.240 15.636 16.877 1.00 70.36 N ANISOU 2199 N ILE A 282 12049 7674 7012 457 315 429 N ATOM 2200 CA ILE A 282 -34.146 14.313 16.263 1.00 70.60 C ANISOU 2200 CA ILE A 282 12358 7494 6973 588 342 438 C ATOM 2201 C ILE A 282 -34.447 14.343 14.746 1.00 67.74 C ANISOU 2201 C ILE A 282 11854 7166 6718 524 306 330 C ATOM 2202 O ILE A 282 -33.820 13.600 13.993 1.00 68.54 O ANISOU 2202 O ILE A 282 12035 7237 6769 729 251 312 O ATOM 2203 CB ILE A 282 -35.041 13.285 17.041 1.00 74.40 C ANISOU 2203 CB ILE A 282 13206 7664 7399 453 517 492 C ATOM 2204 CG1 ILE A 282 -34.228 12.550 18.133 1.00 76.90 C ANISOU 2204 CG1 ILE A 282 13820 7874 7526 700 527 625 C ATOM 2205 CG2 ILE A 282 -35.810 12.238 16.204 1.00 78.44 C ANISOU 2205 CG2 ILE A 282 13913 7943 7947 369 592 427 C ATOM 2206 CD1 ILE A 282 -33.529 13.468 19.146 1.00 78.06 C ANISOU 2206 CD1 ILE A 282 13815 8232 7612 756 467 679 C ATOM 2207 N LEU A 283 -35.387 15.198 14.321 1.00 64.41 N ANISOU 2207 N LEU A 283 11212 6826 6434 256 332 254 N ATOM 2208 CA LEU A 283 -35.808 15.323 12.928 1.00 60.69 C ANISOU 2208 CA LEU A 283 10612 6399 6050 173 300 149 C ATOM 2209 C LEU A 283 -34.843 16.140 12.054 1.00 60.79 C ANISOU 2209 C LEU A 283 10312 6684 6100 301 160 121 C ATOM 2210 O LEU A 283 -34.743 15.830 10.862 1.00 63.05 O ANISOU 2210 O LEU A 283 10495 7028 6434 267 125 42 O ATOM 2211 CB LEU A 283 -37.225 15.932 12.859 1.00 58.10 C ANISOU 2211 CB LEU A 283 10178 6060 5838 -160 382 78 C ATOM 2212 CG LEU A 283 -38.375 14.949 13.160 1.00 62.24 C ANISOU 2212 CG LEU A 283 10987 6317 6346 -361 544 77 C ATOM 2213 CD1 LEU A 283 -39.710 15.704 13.293 1.00 61.00 C ANISOU 2213 CD1 LEU A 283 10656 6212 6310 -690 603 -22 C ATOM 2214 CD2 LEU A 283 -38.474 13.818 12.116 1.00 64.99 C ANISOU 2214 CD2 LEU A 283 11679 6404 6608 -255 586 63 C ATOM 2215 N VAL A 284 -34.176 17.172 12.599 1.00 57.69 N ANISOU 2215 N VAL A 284 9776 6463 5681 434 84 178 N ATOM 2216 CA VAL A 284 -33.333 18.059 11.789 1.00 54.84 C ANISOU 2216 CA VAL A 284 9121 6354 5360 523 -30 152 C ATOM 2217 C VAL A 284 -32.152 17.339 11.110 1.00 56.19 C ANISOU 2217 C VAL A 284 9335 6541 5473 726 -83 120 C ATOM 2218 O VAL A 284 -32.016 17.490 9.905 1.00 56.98 O ANISOU 2218 O VAL A 284 9283 6740 5626 689 -114 57 O ATOM 2219 CB VAL A 284 -32.818 19.338 12.506 1.00 53.22 C ANISOU 2219 CB VAL A 284 8790 6309 5122 622 -95 206 C ATOM 2220 CG1 VAL A 284 -33.955 20.338 12.773 1.00 52.55 C ANISOU 2220 CG1 VAL A 284 8447 6463 5058 735 -202 178 C ATOM 2221 CG2 VAL A 284 -31.989 19.092 13.775 1.00 50.90 C ANISOU 2221 CG2 VAL A 284 8395 6039 4905 417 -45 215 C ATOM 2222 N ASN A 285 -31.382 16.511 11.831 1.00 57.60 N ANISOU 2222 N ASN A 285 9727 6628 5531 961 -92 164 N ATOM 2223 CA ASN A 285 -30.184 15.854 11.275 1.00 56.97 C ANISOU 2223 CA ASN A 285 9681 6579 5386 1199 -139 132 C ATOM 2224 C ASN A 285 -30.462 14.924 10.062 1.00 61.11 C ANISOU 2224 C ASN A 285 10342 6943 5935 1118 -77 50 C ATOM 2225 O ASN A 285 -29.793 15.095 9.035 1.00 59.95 O ANISOU 2225 O ASN A 285 10050 6928 5800 1181 -122 -14 O ATOM 2226 CB ASN A 285 -29.365 15.176 12.412 1.00 59.63 C ANISOU 2226 CB ASN A 285 10237 6841 5577 1492 -159 204 C ATOM 2227 CG ASN A 285 -28.591 16.159 13.294 1.00 62.55 C ANISOU 2227 CG ASN A 285 10402 7464 5900 1631 -264 249 C ATOM 2228 ND2 ASN A 285 -28.112 15.731 14.456 1.00 63.02 N ANISOU 2228 ND2 ASN A 285 10600 7525 5819 1924 -310 305 N ATOM 2229 OD1 ASN A 285 -28.393 17.308 12.924 1.00 64.09 O ANISOU 2229 OD1 ASN A 285 10323 7850 6180 1480 -303 230 O ATOM 2230 N PRO A 286 -31.466 14.014 10.123 1.00 63.50 N ANISOU 2230 N PRO A 286 10918 6972 6239 971 29 40 N ATOM 2231 CA PRO A 286 -31.961 13.304 8.926 1.00 63.30 C ANISOU 2231 CA PRO A 286 11012 6807 6234 874 80 -65 C ATOM 2232 C PRO A 286 -32.469 14.203 7.785 1.00 64.89 C ANISOU 2232 C PRO A 286 10921 7200 6534 674 40 -149 C ATOM 2233 O PRO A 286 -32.122 13.962 6.630 1.00 70.14 O ANISOU 2233 O PRO A 286 11548 7920 7184 731 13 -231 O ATOM 2234 CB PRO A 286 -33.078 12.390 9.464 1.00 52.52 C ANISOU 2234 CB PRO A 286 9959 5130 4866 686 211 -58 C ATOM 2235 CG PRO A 286 -32.708 12.154 10.916 1.00 67.31 C ANISOU 2235 CG PRO A 286 11981 6935 6660 830 227 72 C ATOM 2236 CD PRO A 286 -32.104 13.488 11.331 1.00 64.44 C ANISOU 2236 CD PRO A 286 11275 6885 6325 891 117 115 C ATOM 2237 N THR A 287 -33.293 15.209 8.098 1.00 62.88 N ANISOU 2237 N THR A 287 10464 7056 6371 460 37 -129 N ATOM 2238 CA THR A 287 -33.914 16.031 7.062 1.00 60.63 C ANISOU 2238 CA THR A 287 9908 6959 6170 298 -6 -192 C ATOM 2239 C THR A 287 -32.948 17.074 6.457 1.00 61.07 C ANISOU 2239 C THR A 287 9712 7272 6219 460 -103 -173 C ATOM 2240 O THR A 287 -33.035 17.321 5.255 1.00 61.98 O ANISOU 2240 O THR A 287 9673 7520 6355 410 -138 -229 O ATOM 2241 CB THR A 287 -35.196 16.721 7.577 1.00 57.95 C ANISOU 2241 CB THR A 287 9423 6670 5927 59 21 -170 C ATOM 2242 CG2 THR A 287 -36.307 15.722 7.935 1.00 57.04 C ANISOU 2242 CG2 THR A 287 9540 6315 5816 -127 136 -189 C ATOM 2243 OG1 THR A 287 -34.964 17.534 8.710 1.00 58.98 O ANISOU 2243 OG1 THR A 287 9431 6910 6067 143 -11 -77 O ATOM 2244 N SER A 288 -32.005 17.624 7.233 1.00 61.51 N ANISOU 2244 N SER A 288 9721 7411 6239 644 -143 -97 N ATOM 2245 CA SER A 288 -31.004 18.565 6.742 1.00 59.79 C ANISOU 2245 CA SER A 288 9266 7438 6013 781 -220 -87 C ATOM 2246 C SER A 288 -30.017 17.869 5.791 1.00 61.59 C ANISOU 2246 C SER A 288 9553 7683 6166 953 -229 -150 C ATOM 2247 O SER A 288 -29.742 18.405 4.726 1.00 60.86 O ANISOU 2247 O SER A 288 9274 7767 6082 953 -260 -183 O ATOM 2248 CB SER A 288 -30.337 19.312 7.920 1.00 59.09 C ANISOU 2248 CB SER A 288 9118 7443 5891 929 -264 -14 C ATOM 2249 OG SER A 288 -29.383 18.536 8.631 1.00 60.99 O ANISOU 2249 OG SER A 288 9261 7711 6202 771 -258 30 O ATOM 2250 N SER A 289 -29.565 16.651 6.128 1.00 62.59 N ANISOU 2250 N SER A 289 9952 7620 6209 1111 -194 -164 N ATOM 2251 CA SER A 289 -28.704 15.848 5.254 1.00 62.27 C ANISOU 2251 CA SER A 289 9992 7578 6090 1301 -191 -233 C ATOM 2252 C SER A 289 -29.374 15.466 3.910 1.00 62.18 C ANISOU 2252 C SER A 289 9982 7542 6100 1132 -165 -335 C ATOM 2253 O SER A 289 -28.711 15.521 2.874 1.00 61.62 O ANISOU 2253 O SER A 289 9837 7594 5982 1237 -180 -396 O ATOM 2254 CB SER A 289 -28.114 14.663 6.047 1.00 65.83 C ANISOU 2254 CB SER A 289 10782 7783 6449 1505 -146 -224 C ATOM 2255 OG SER A 289 -29.112 13.830 6.601 1.00 65.79 O ANISOU 2255 OG SER A 289 11048 7487 6464 1317 -63 -246 O ATOM 2256 N LEU A 290 -30.689 15.202 3.928 1.00 62.53 N ANISOU 2256 N LEU A 290 10098 7454 6208 868 -127 -362 N ATOM 2257 CA LEU A 290 -31.550 15.093 2.747 1.00 62.90 C ANISOU 2257 CA LEU A 290 10111 7519 6269 688 -122 -468 C ATOM 2258 C LEU A 290 -31.651 16.415 1.955 1.00 64.47 C ANISOU 2258 C LEU A 290 9983 8011 6502 641 -188 -452 C ATOM 2259 O LEU A 290 -31.700 16.373 0.726 1.00 69.51 O ANISOU 2259 O LEU A 290 10568 8753 7092 656 -205 -526 O ATOM 2260 CB LEU A 290 -32.925 14.546 3.202 1.00 60.35 C ANISOU 2260 CB LEU A 290 9894 7027 6010 406 -70 -502 C ATOM 2261 CG LEU A 290 -34.032 14.441 2.127 1.00 61.50 C ANISOU 2261 CG LEU A 290 9971 7223 6171 186 -80 -622 C ATOM 2262 CD1 LEU A 290 -33.625 13.601 0.900 1.00 64.27 C ANISOU 2262 CD1 LEU A 290 10518 7473 6427 270 -59 -749 C ATOM 2263 CD2 LEU A 290 -35.341 13.925 2.745 1.00 61.61 C ANISOU 2263 CD2 LEU A 290 10042 7110 6257 -100 -28 -652 C ATOM 2264 N ALA A 291 -31.693 17.570 2.631 1.00 60.32 N ANISOU 2264 N ALA A 291 9257 7613 6050 586 -219 -355 N ATOM 2265 CA ALA A 291 -31.691 18.880 1.972 1.00 60.47 C ANISOU 2265 CA ALA A 291 8995 7880 6099 552 -269 -322 C ATOM 2266 C ALA A 291 -30.348 19.162 1.283 1.00 63.23 C ANISOU 2266 C ALA A 291 9249 8393 6383 766 -289 -309 C ATOM 2267 O ALA A 291 -30.311 19.540 0.115 1.00 65.34 O ANISOU 2267 O ALA A 291 9365 8834 6627 762 -306 -320 O ATOM 2268 CB ALA A 291 -32.070 19.986 2.964 1.00 61.00 C ANISOU 2268 CB ALA A 291 8906 8008 6264 445 -284 -230 C ATOM 2269 N PHE A 292 -29.260 18.892 2.008 1.00 64.15 N ANISOU 2269 N PHE A 292 9445 8471 6460 960 -284 -283 N ATOM 2270 CA PHE A 292 -27.879 19.056 1.560 1.00 62.83 C ANISOU 2270 CA PHE A 292 9169 8478 6223 1175 -298 -286 C ATOM 2271 C PHE A 292 -27.524 18.141 0.372 1.00 65.43 C ANISOU 2271 C PHE A 292 9605 8793 6463 1269 -269 -385 C ATOM 2272 O PHE A 292 -26.737 18.537 -0.489 1.00 67.16 O ANISOU 2272 O PHE A 292 9674 9210 6632 1360 -268 -402 O ATOM 2273 CB PHE A 292 -26.946 18.813 2.765 1.00 62.98 C ANISOU 2273 CB PHE A 292 9253 8471 6205 1385 -311 -246 C ATOM 2274 CG PHE A 292 -27.164 19.692 3.998 1.00 63.45 C ANISOU 2274 CG PHE A 292 9183 8596 6329 1318 -347 -162 C ATOM 2275 CD1 PHE A 292 -27.904 20.899 3.952 1.00 62.03 C ANISOU 2275 CD1 PHE A 292 8849 8475 6246 1093 -353 -124 C ATOM 2276 CD2 PHE A 292 -26.568 19.316 5.221 1.00 62.76 C ANISOU 2276 CD2 PHE A 292 9132 8518 6195 1497 -377 -125 C ATOM 2277 CE1 PHE A 292 -28.121 21.631 5.109 1.00 59.72 C ANISOU 2277 CE1 PHE A 292 8456 8228 6007 1034 -378 -62 C ATOM 2278 CE2 PHE A 292 -26.785 20.070 6.366 1.00 62.36 C ANISOU 2278 CE2 PHE A 292 8970 8536 6187 1431 -413 -65 C ATOM 2279 CZ PHE A 292 -27.572 21.214 6.311 1.00 60.47 C ANISOU 2279 CZ PHE A 292 8591 8336 6051 1193 -408 -39 C ATOM 2280 N PHE A 293 -28.158 16.961 0.309 1.00 64.81 N ANISOU 2280 N PHE A 293 9790 8476 6358 1234 -235 -459 N ATOM 2281 CA PHE A 293 -28.088 16.004 -0.796 1.00 65.21 C ANISOU 2281 CA PHE A 293 9984 8477 6317 1315 -202 -577 C ATOM 2282 C PHE A 293 -28.603 16.545 -2.148 1.00 66.40 C ANISOU 2282 C PHE A 293 9974 8806 6450 1179 -219 -624 C ATOM 2283 O PHE A 293 -28.235 15.992 -3.180 1.00 70.86 O ANISOU 2283 O PHE A 293 10578 9427 6918 1282 -197 -712 O ATOM 2284 CB PHE A 293 -28.733 14.676 -0.327 1.00 67.12 C ANISOU 2284 CB PHE A 293 10555 8398 6549 1244 -154 -651 C ATOM 2285 CG PHE A 293 -28.889 13.552 -1.336 1.00 69.33 C ANISOU 2285 CG PHE A 293 11026 8583 6735 1306 -114 -795 C ATOM 2286 CD1 PHE A 293 -27.783 12.744 -1.677 1.00 70.29 C ANISOU 2286 CD1 PHE A 293 11252 8693 6761 1606 -83 -832 C ATOM 2287 CD2 PHE A 293 -30.104 13.380 -2.032 1.00 68.71 C ANISOU 2287 CD2 PHE A 293 11020 8431 6656 1068 -107 -904 C ATOM 2288 CE1 PHE A 293 -27.911 11.764 -2.652 1.00 72.30 C ANISOU 2288 CE1 PHE A 293 11700 8847 6923 1671 -36 -976 C ATOM 2289 CE2 PHE A 293 -30.213 12.389 -2.999 1.00 70.76 C ANISOU 2289 CE2 PHE A 293 11468 8599 6820 1111 -70 -1056 C ATOM 2290 CZ PHE A 293 -29.123 11.586 -3.307 1.00 72.69 C ANISOU 2290 CZ PHE A 293 11837 8812 6971 1414 -29 -1092 C ATOM 2291 N ASN A 294 -29.361 17.657 -2.149 1.00 63.79 N ANISOU 2291 N ASN A 294 9470 8569 6199 969 -255 -564 N ATOM 2292 CA ASN A 294 -29.767 18.370 -3.368 1.00 61.88 C ANISOU 2292 CA ASN A 294 9076 8509 5927 861 -280 -585 C ATOM 2293 C ASN A 294 -28.553 18.885 -4.168 1.00 60.26 C ANISOU 2293 C ASN A 294 8690 8547 5661 1008 -271 -545 C ATOM 2294 O ASN A 294 -28.560 18.792 -5.394 1.00 60.03 O ANISOU 2294 O ASN A 294 8601 8657 5552 988 -270 -584 O ATOM 2295 CB ASN A 294 -30.691 19.565 -3.030 1.00 62.44 C ANISOU 2295 CB ASN A 294 9001 8627 6098 646 -320 -511 C ATOM 2296 CG ASN A 294 -31.654 20.013 -4.139 1.00 63.84 C ANISOU 2296 CG ASN A 294 9033 8993 6232 556 -354 -515 C ATOM 2297 ND2 ASN A 294 -31.255 20.044 -5.404 1.00 65.60 N ANISOU 2297 ND2 ASN A 294 9356 9183 6387 468 -370 -634 N ATOM 2298 OD1 ASN A 294 -32.782 20.390 -3.851 1.00 63.23 O ANISOU 2298 OD1 ASN A 294 8765 9087 6172 563 -365 -414 O ATOM 2299 N SER A 295 -27.519 19.392 -3.481 1.00 62.27 N ANISOU 2299 N SER A 295 8851 8868 5940 1149 -261 -473 N ATOM 2300 CA SER A 295 -26.316 19.947 -4.109 1.00 63.55 C ANISOU 2300 CA SER A 295 8816 9277 6053 1261 -238 -439 C ATOM 2301 C SER A 295 -25.546 18.949 -4.995 1.00 62.72 C ANISOU 2301 C SER A 295 8792 9222 5815 1451 -192 -542 C ATOM 2302 O SER A 295 -25.038 19.356 -6.039 1.00 63.14 O ANISOU 2302 O SER A 295 8687 9498 5806 1514 -157 -532 O ATOM 2303 CB SER A 295 -25.400 20.560 -3.030 1.00 63.88 C ANISOU 2303 CB SER A 295 8724 9397 6153 1350 -245 -360 C ATOM 2304 OG SER A 295 -25.882 21.829 -2.636 1.00 65.38 O ANISOU 2304 OG SER A 295 8799 9589 6453 1173 -275 -266 O ATOM 2305 N CYS A 296 -25.503 17.665 -4.595 1.00 64.58 N ANISOU 2305 N CYS A 296 9282 9251 6006 1543 -179 -643 N ATOM 2306 CA CYS A 296 -24.865 16.592 -5.365 1.00 67.60 C ANISOU 2306 CA CYS A 296 9774 9652 6259 1733 -128 -759 C ATOM 2307 C CYS A 296 -25.770 16.004 -6.472 1.00 66.76 C ANISOU 2307 C CYS A 296 9828 9458 6081 1609 -124 -878 C ATOM 2308 O CYS A 296 -25.243 15.290 -7.324 1.00 69.40 O ANISOU 2308 O CYS A 296 10245 9832 6293 1742 -78 -987 O ATOM 2309 CB CYS A 296 -24.248 15.514 -4.446 1.00 71.73 C ANISOU 2309 CB CYS A 296 10496 9999 6760 1976 -104 -799 C ATOM 2310 SG CYS A 296 -25.452 14.344 -3.758 1.00 74.62 S ANISOU 2310 SG CYS A 296 11238 9957 7156 1882 -101 -865 S ATOM 2311 N LEU A 297 -27.080 16.321 -6.469 1.00 65.67 N ANISOU 2311 N LEU A 297 9723 9219 6008 1360 -171 -872 N ATOM 2312 CA LEU A 297 -28.028 15.943 -7.526 1.00 67.31 C ANISOU 2312 CA LEU A 297 10034 9398 6142 1214 -186 -993 C ATOM 2313 C LEU A 297 -28.037 16.938 -8.699 1.00 71.04 C ANISOU 2313 C LEU A 297 10292 10146 6552 1135 -212 -952 C ATOM 2314 O LEU A 297 -28.384 16.533 -9.808 1.00 73.87 O ANISOU 2314 O LEU A 297 10714 10565 6791 1099 -217 -1062 O ATOM 2315 CB LEU A 297 -29.459 15.841 -6.956 1.00 64.88 C ANISOU 2315 CB LEU A 297 9836 8891 5926 977 -224 -1017 C ATOM 2316 CG LEU A 297 -29.699 14.685 -5.964 1.00 65.64 C ANISOU 2316 CG LEU A 297 10224 8663 6052 993 -183 -1090 C ATOM 2317 CD1 LEU A 297 -31.051 14.878 -5.242 1.00 64.68 C ANISOU 2317 CD1 LEU A 297 10161 8401 6013 707 -210 -1120 C ATOM 2318 CD2 LEU A 297 -29.570 13.301 -6.637 1.00 69.06 C ANISOU 2318 CD2 LEU A 297 10900 8979 6359 1133 -127 -1253 C ATOM 2319 N ASN A 298 -27.677 18.209 -8.442 1.00 72.92 N ANISOU 2319 N ASN A 298 10299 10547 6862 1108 -226 -796 N ATOM 2320 CA ASN A 298 -27.744 19.319 -9.401 1.00 75.84 C ANISOU 2320 CA ASN A 298 10490 11153 7172 1034 -241 -730 C ATOM 2321 C ASN A 298 -26.909 19.187 -10.701 1.00 81.08 C ANISOU 2321 C ASN A 298 11143 11997 7668 1174 -183 -790 C ATOM 2322 O ASN A 298 -27.391 19.691 -11.718 1.00 82.64 O ANISOU 2322 O ASN A 298 11300 12339 7761 1099 -204 -797 O ATOM 2323 CB ASN A 298 -27.461 20.660 -8.685 1.00 72.47 C ANISOU 2323 CB ASN A 298 9849 10829 6857 992 -242 -554 C ATOM 2324 CG ASN A 298 -28.527 21.090 -7.666 1.00 71.95 C ANISOU 2324 CG ASN A 298 9773 10628 6936 830 -301 -493 C ATOM 2325 ND2 ASN A 298 -28.165 22.012 -6.775 1.00 71.78 N ANISOU 2325 ND2 ASN A 298 9631 10614 7028 824 -293 -375 N ATOM 2326 OD1 ASN A 298 -29.661 20.617 -7.683 1.00 72.48 O ANISOU 2326 OD1 ASN A 298 9932 10598 7009 704 -349 -560 O ATOM 2327 N PRO A 299 -25.762 18.461 -10.720 1.00 82.80 N ANISOU 2327 N PRO A 299 11382 12236 7841 1384 -110 -830 N ATOM 2328 CA PRO A 299 -25.092 18.078 -11.980 1.00 85.49 C ANISOU 2328 CA PRO A 299 11724 12751 8007 1517 -43 -908 C ATOM 2329 C PRO A 299 -25.950 17.221 -12.924 1.00 86.54 C ANISOU 2329 C PRO A 299 12059 12816 8008 1475 -64 -1076 C ATOM 2330 O PRO A 299 -25.980 17.506 -14.117 1.00 89.24 O ANISOU 2330 O PRO A 299 12364 13344 8199 1469 -47 -1104 O ATOM 2331 CB PRO A 299 -23.825 17.333 -11.526 1.00 88.59 C ANISOU 2331 CB PRO A 299 12130 13131 8397 1767 29 -945 C ATOM 2332 CG PRO A 299 -23.534 17.904 -10.153 1.00 86.85 C ANISOU 2332 CG PRO A 299 11785 12873 8341 1743 0 -816 C ATOM 2333 CD PRO A 299 -24.924 18.114 -9.573 1.00 83.85 C ANISOU 2333 CD PRO A 299 11485 12304 8069 1523 -85 -784 C ATOM 2334 N MET A 300 -26.641 16.207 -12.378 1.00 86.51 N ANISOU 2334 N MET A 300 12276 12547 8046 1434 -96 -1192 N ATOM 2335 CA MET A 300 -27.477 15.278 -13.141 1.00 89.07 C ANISOU 2335 CA MET A 300 12800 12796 8247 1363 -116 -1377 C ATOM 2336 C MET A 300 -28.845 15.866 -13.529 1.00 88.69 C ANISOU 2336 C MET A 300 12674 12834 8190 1113 -214 -1360 C ATOM 2337 O MET A 300 -29.354 15.508 -14.590 1.00 92.11 O ANISOU 2337 O MET A 300 13149 13384 8466 1064 -240 -1468 O ATOM 2338 CB MET A 300 -27.649 13.953 -12.367 1.00 93.59 C ANISOU 2338 CB MET A 300 13653 13037 8870 1379 -101 -1511 C ATOM 2339 CG MET A 300 -26.323 13.262 -11.993 1.00 99.36 C ANISOU 2339 CG MET A 300 14543 13679 9530 1664 -4 -1601 C ATOM 2340 SD MET A 300 -25.599 13.746 -10.400 1.00102.15 S ANISOU 2340 SD MET A 300 14788 14015 10011 1889 35 -1441 S ATOM 2341 CE MET A 300 -26.629 12.760 -9.279 1.00100.32 C ANISOU 2341 CE MET A 300 14748 13429 9940 1738 -10 -1418 C ATOM 2342 N LEU A 301 -29.408 16.745 -12.680 1.00 86.77 N ANISOU 2342 N LEU A 301 12314 12550 8105 968 -273 -1231 N ATOM 2343 CA LEU A 301 -30.707 17.389 -12.890 1.00 85.50 C ANISOU 2343 CA LEU A 301 12073 12466 7947 752 -372 -1218 C ATOM 2344 C LEU A 301 -30.679 18.453 -13.997 1.00 81.85 C ANISOU 2344 C LEU A 301 11433 12299 7366 765 -394 -1117 C ATOM 2345 O LEU A 301 -31.554 18.432 -14.863 1.00 81.65 O ANISOU 2345 O LEU A 301 11406 12397 7219 670 -466 -1185 O ATOM 2346 CB LEU A 301 -31.190 18.036 -11.571 1.00 84.81 C ANISOU 2346 CB LEU A 301 11903 12263 8058 623 -412 -1102 C ATOM 2347 CG LEU A 301 -31.754 17.058 -10.522 1.00 86.80 C ANISOU 2347 CG LEU A 301 12341 12218 8421 560 -395 -1187 C ATOM 2348 CD1 LEU A 301 -31.931 17.767 -9.168 1.00 85.41 C ANISOU 2348 CD1 LEU A 301 12068 11960 8424 534 -392 -1030 C ATOM 2349 CD2 LEU A 301 -33.069 16.398 -10.985 1.00 89.03 C ANISOU 2349 CD2 LEU A 301 12717 12430 8680 340 -457 -1341 C ATOM 2350 N TYR A 302 -29.716 19.387 -13.912 1.00 80.32 N ANISOU 2350 N TYR A 302 11093 12226 7198 877 -331 -956 N ATOM 2351 CA TYR A 302 -29.722 20.621 -14.700 1.00 81.27 C ANISOU 2351 CA TYR A 302 11054 12594 7232 871 -335 -817 C ATOM 2352 C TYR A 302 -28.705 20.615 -15.850 1.00 83.00 C ANISOU 2352 C TYR A 302 11281 12997 7257 1017 -247 -849 C ATOM 2353 O TYR A 302 -29.005 21.209 -16.884 1.00 83.83 O ANISOU 2353 O TYR A 302 11377 13284 7189 998 -272 -852 O ATOM 2354 CB TYR A 302 -29.498 21.833 -13.764 1.00 79.35 C ANISOU 2354 CB TYR A 302 10640 12361 7149 853 -311 -609 C ATOM 2355 CG TYR A 302 -30.589 22.009 -12.718 1.00 78.27 C ANISOU 2355 CG TYR A 302 10463 12104 7173 704 -397 -551 C ATOM 2356 CD1 TYR A 302 -30.416 21.505 -11.412 1.00 78.10 C ANISOU 2356 CD1 TYR A 302 10509 11862 7305 669 -404 -598 C ATOM 2357 CD2 TYR A 302 -31.805 22.636 -13.060 1.00 78.48 C ANISOU 2357 CD2 TYR A 302 10388 12242 7188 614 -466 -445 C ATOM 2358 CE1 TYR A 302 -31.467 21.572 -10.479 1.00 78.90 C ANISOU 2358 CE1 TYR A 302 10568 11866 7546 533 -467 -549 C ATOM 2359 CE2 TYR A 302 -32.853 22.717 -12.121 1.00 77.76 C ANISOU 2359 CE2 TYR A 302 10246 12057 7243 497 -536 -399 C ATOM 2360 CZ TYR A 302 -32.693 22.161 -10.837 1.00 78.92 C ANISOU 2360 CZ TYR A 302 10450 11994 7542 448 -531 -456 C ATOM 2361 OH TYR A 302 -33.722 22.174 -9.941 1.00 79.76 O ANISOU 2361 OH TYR A 302 10500 12019 7786 330 -586 -415 O ATOM 2362 N VAL A 303 -27.535 19.980 -15.663 1.00 82.01 N ANISOU 2362 N VAL A 303 11167 12847 7145 1174 -144 -873 N ATOM 2363 CA VAL A 303 -26.388 20.155 -16.558 1.00 83.37 C ANISOU 2363 CA VAL A 303 11304 13223 7151 1320 -36 -882 C ATOM 2364 C VAL A 303 -26.226 18.951 -17.503 1.00 86.67 C ANISOU 2364 C VAL A 303 11916 13624 7390 1406 -22 -1103 C ATOM 2365 O VAL A 303 -26.448 19.098 -18.704 1.00 90.32 O ANISOU 2365 O VAL A 303 12408 14254 7656 1392 -28 -1149 O ATOM 2366 CB VAL A 303 -25.065 20.378 -15.769 1.00 83.07 C ANISOU 2366 CB VAL A 303 11149 13210 7203 1457 70 -814 C ATOM 2367 CG1 VAL A 303 -23.892 20.769 -16.691 1.00 82.32 C ANISOU 2367 CG1 VAL A 303 10955 13376 6947 1569 196 -784 C ATOM 2368 CG2 VAL A 303 -25.256 21.415 -14.650 1.00 81.46 C ANISOU 2368 CG2 VAL A 303 10792 12959 7199 1350 42 -636 C ATOM 2369 N PHE A 304 -25.863 17.786 -16.941 1.00 88.57 N ANISOU 2369 N PHE A 304 12308 13657 7688 1501 0 -1242 N ATOM 2370 CA PHE A 304 -25.600 16.534 -17.654 1.00 91.18 C ANISOU 2370 CA PHE A 304 12848 13939 7859 1617 41 -1462 C ATOM 2371 C PHE A 304 -26.866 15.784 -18.109 1.00 90.22 C ANISOU 2371 C PHE A 304 12907 13698 7673 1449 -61 -1625 C ATOM 2372 O PHE A 304 -26.734 14.754 -18.770 1.00 90.71 O ANISOU 2372 O PHE A 304 13187 13651 7628 1513 -32 -1835 O ATOM 2373 CB PHE A 304 -24.661 15.648 -16.805 1.00 93.33 C ANISOU 2373 CB PHE A 304 13231 14018 8212 1813 114 -1537 C ATOM 2374 CG PHE A 304 -23.286 16.249 -16.546 1.00 95.49 C ANISOU 2374 CG PHE A 304 13317 14465 8499 2009 220 -1430 C ATOM 2375 CD1 PHE A 304 -22.456 16.621 -17.625 1.00 97.05 C ANISOU 2375 CD1 PHE A 304 13384 14954 8537 2081 308 -1402 C ATOM 2376 CD2 PHE A 304 -22.810 16.420 -15.228 1.00 95.45 C ANISOU 2376 CD2 PHE A 304 13256 14354 8658 2111 234 -1360 C ATOM 2377 CE1 PHE A 304 -21.207 17.179 -17.385 1.00 98.85 C ANISOU 2377 CE1 PHE A 304 13414 15365 8780 2235 415 -1314 C ATOM 2378 CE2 PHE A 304 -21.549 16.962 -15.009 1.00 97.65 C ANISOU 2378 CE2 PHE A 304 13330 14828 8945 2278 323 -1278 C ATOM 2379 CZ PHE A 304 -20.756 17.347 -16.083 1.00 99.47 C ANISOU 2379 CZ PHE A 304 13415 15350 9028 2330 417 -1259 C ATOM 2380 N ALA A 305 -28.059 16.338 -17.817 1.00 90.97 N ANISOU 2380 N ALA A 305 12917 13818 7831 1237 -175 -1545 N ATOM 2381 CA ALA A 305 -29.321 16.000 -18.480 1.00 97.80 C ANISOU 2381 CA ALA A 305 13891 14668 8598 1065 -281 -1701 C ATOM 2382 C ALA A 305 -29.321 16.395 -19.970 1.00106.51 C ANISOU 2382 C ALA A 305 14960 16060 9449 1079 -299 -1732 C ATOM 2383 O ALA A 305 -29.924 15.687 -20.777 1.00106.67 O ANISOU 2383 O ALA A 305 15079 16110 9339 962 -386 -1899 O ATOM 2384 CB ALA A 305 -30.482 16.692 -17.747 1.00 94.40 C ANISOU 2384 CB ALA A 305 13359 14182 8328 850 -399 -1609 C ATOM 2385 N GLY A 306 -28.604 17.484 -20.308 1.00114.24 N ANISOU 2385 N GLY A 306 15802 17257 10348 1211 -216 -1580 N ATOM 2386 CA GLY A 306 -28.361 17.931 -21.676 1.00122.57 C ANISOU 2386 CA GLY A 306 16835 18592 11144 1243 -212 -1583 C ATOM 2387 C GLY A 306 -27.321 17.017 -22.335 1.00128.90 C ANISOU 2387 C GLY A 306 17757 19457 11764 1433 -80 -1729 C ATOM 2388 O GLY A 306 -26.328 16.635 -21.711 1.00132.41 O ANISOU 2388 O GLY A 306 18246 19770 12296 1579 26 -1770 O ATOM 2389 N GLN A 307 -27.568 16.689 -23.613 1.00127.21 N ANISOU 2389 N GLN A 307 17591 19463 11279 1445 -90 -1807 N ATOM 2390 CA GLN A 307 -26.753 15.814 -24.458 1.00134.65 C ANISOU 2390 CA GLN A 307 18667 20477 12015 1620 33 -1979 C ATOM 2391 C GLN A 307 -25.334 16.360 -24.687 1.00136.57 C ANISOU 2391 C GLN A 307 18764 20896 12231 1799 206 -1820 C ATOM 2392 O GLN A 307 -24.374 15.596 -24.600 1.00137.76 O ANISOU 2392 O GLN A 307 18973 21006 12363 1986 339 -1924 O ATOM 2393 CB GLN A 307 -27.452 15.590 -25.824 1.00140.10 C ANISOU 2393 CB GLN A 307 19461 21366 12406 1567 -37 -2121 C ATOM 2394 CG GLN A 307 -28.792 14.817 -25.793 1.00144.49 C ANISOU 2394 CG GLN A 307 20150 21789 12962 1371 -208 -2321 C ATOM 2395 CD GLN A 307 -30.023 15.625 -25.357 1.00145.35 C ANISOU 2395 CD GLN A 307 20096 21952 13177 1179 -371 -2160 C ATOM 2396 NE2 GLN A 307 -31.125 14.928 -25.075 1.00147.55 N ANISOU 2396 NE2 GLN A 307 20446 22188 13430 994 -526 -2332 N ATOM 2397 OE1 GLN A 307 -29.999 16.853 -25.288 1.00143.08 O ANISOU 2397 OE1 GLN A 307 19621 21749 12994 1195 -355 -1892 O ATOM 2398 N ASP A 308 -25.256 17.675 -24.949 1.00137.21 N ANISOU 2398 N ASP A 308 18655 21170 12309 1744 215 -1571 N ATOM 2399 CA ASP A 308 -24.053 18.457 -25.240 1.00137.59 C ANISOU 2399 CA ASP A 308 18558 21417 12303 1871 392 -1427 C ATOM 2400 C ASP A 308 -23.017 18.449 -24.102 1.00136.38 C ANISOU 2400 C ASP A 308 18302 21132 12384 1972 486 -1387 C ATOM 2401 O ASP A 308 -21.829 18.307 -24.384 1.00137.58 O ANISOU 2401 O ASP A 308 18394 21404 12475 2141 646 -1410 O ATOM 2402 CB ASP A 308 -24.351 19.914 -25.692 1.00137.94 C ANISOU 2402 CB ASP A 308 18450 21645 12314 1762 383 -1159 C ATOM 2403 CG ASP A 308 -25.362 20.736 -24.867 1.00137.94 C ANISOU 2403 CG ASP A 308 18367 21483 12560 1602 247 -1011 C ATOM 2404 OD1 ASP A 308 -26.118 20.153 -24.058 1.00138.07 O ANISOU 2404 OD1 ASP A 308 18477 21322 12663 1517 101 -1135 O ATOM 2405 OD2 ASP A 308 -25.387 21.964 -25.099 1.00137.75 O1- ANISOU 2405 OD2 ASP A 308 18188 21509 12641 1554 297 -777 O1- ATOM 2406 N PHE A 309 -23.479 18.576 -22.847 1.00127.80 N ANISOU 2406 N PHE A 309 17186 19818 11556 1877 388 -1331 N ATOM 2407 CA PHE A 309 -22.633 18.512 -21.651 1.00120.28 C ANISOU 2407 CA PHE A 309 16129 18759 10814 1973 457 -1283 C ATOM 2408 C PHE A 309 -22.107 17.094 -21.379 1.00115.75 C ANISOU 2408 C PHE A 309 15717 18031 10231 2166 504 -1504 C ATOM 2409 O PHE A 309 -20.951 16.947 -20.984 1.00114.88 O ANISOU 2409 O PHE A 309 15517 17966 10165 2349 618 -1503 O ATOM 2410 CB PHE A 309 -23.412 19.020 -20.422 1.00119.95 C ANISOU 2410 CB PHE A 309 16023 18524 11029 1818 340 -1158 C ATOM 2411 CG PHE A 309 -23.804 20.483 -20.474 1.00122.14 C ANISOU 2411 CG PHE A 309 16153 18919 11337 1653 301 -935 C ATOM 2412 CD1 PHE A 309 -22.897 21.480 -20.060 1.00123.81 C ANISOU 2412 CD1 PHE A 309 16164 19259 11619 1650 403 -747 C ATOM 2413 CD2 PHE A 309 -25.014 20.866 -21.087 1.00123.05 C ANISOU 2413 CD2 PHE A 309 16330 19014 11409 1503 164 -918 C ATOM 2414 CE1 PHE A 309 -23.234 22.820 -20.198 1.00124.05 C ANISOU 2414 CE1 PHE A 309 16095 19359 11678 1504 380 -539 C ATOM 2415 CE2 PHE A 309 -25.325 22.210 -21.232 1.00123.23 C ANISOU 2415 CE2 PHE A 309 16234 19131 11455 1386 130 -705 C ATOM 2416 CZ PHE A 309 -24.443 23.182 -20.780 1.00123.47 C ANISOU 2416 CZ PHE A 309 16102 19254 11558 1389 243 -512 C ATOM 2417 N ARG A 310 -22.975 16.088 -21.583 1.00112.57 N ANISOU 2417 N ARG A 310 15555 17447 9769 2130 419 -1698 N ATOM 2418 CA ARG A 310 -22.703 14.683 -21.290 1.00112.70 C ANISOU 2418 CA ARG A 310 15773 17242 9805 2302 459 -1900 C ATOM 2419 C ARG A 310 -21.685 14.048 -22.256 1.00115.78 C ANISOU 2419 C ARG A 310 16207 17795 9987 2546 613 -2032 C ATOM 2420 O ARG A 310 -20.829 13.293 -21.799 1.00116.66 O ANISOU 2420 O ARG A 310 16364 17819 10141 2778 702 -2110 O ATOM 2421 CB ARG A 310 -24.041 13.916 -21.253 1.00113.09 C ANISOU 2421 CB ARG A 310 16081 17037 9850 2157 340 -2080 C ATOM 2422 CG ARG A 310 -23.922 12.483 -20.703 1.00114.23 C ANISOU 2422 CG ARG A 310 16479 16876 10049 2306 380 -2268 C ATOM 2423 CD ARG A 310 -25.271 11.783 -20.477 1.00113.67 C ANISOU 2423 CD ARG A 310 16617 16499 10074 2094 261 -2378 C ATOM 2424 NE ARG A 310 -26.078 11.683 -21.701 1.00115.74 N ANISOU 2424 NE ARG A 310 16995 16822 10159 1915 185 -2538 N ATOM 2425 CZ ARG A 310 -27.090 12.489 -22.066 1.00115.73 C ANISOU 2425 CZ ARG A 310 16883 16924 10166 1662 52 -2469 C ATOM 2426 NH1 ARG A 310 -27.494 13.512 -21.302 1.00114.17 N1+ ANISOU 2426 NH1 ARG A 310 16473 16755 10150 1560 -7 -2240 N1+ ATOM 2427 NH2 ARG A 310 -27.718 12.255 -23.224 1.00117.20 N1+ ANISOU 2427 NH2 ARG A 310 17169 17193 10170 1520 -25 -2636 N1+ ATOM 2428 N GLU A 311 -21.773 14.386 -23.555 1.00115.91 N ANISOU 2428 N GLU A 311 16213 18059 9767 2516 648 -2056 N ATOM 2429 CA GLU A 311 -20.826 13.936 -24.579 1.00116.85 C ANISOU 2429 CA GLU A 311 16375 18355 9670 2744 807 -2188 C ATOM 2430 C GLU A 311 -19.472 14.662 -24.471 1.00115.51 C ANISOU 2430 C GLU A 311 15922 18469 9498 2863 961 -2018 C ATOM 2431 O GLU A 311 -18.446 14.022 -24.693 1.00118.74 O ANISOU 2431 O GLU A 311 16316 18986 9813 3108 1111 -2118 O ATOM 2432 CB GLU A 311 -21.473 14.052 -25.977 1.00117.39 C ANISOU 2432 CB GLU A 311 16580 18570 9452 2667 786 -2311 C ATOM 2433 CG GLU A 311 -21.619 15.485 -26.532 1.00116.25 C ANISOU 2433 CG GLU A 311 16284 18652 9234 2463 718 -2111 C ATOM 2434 CD GLU A 311 -22.433 15.536 -27.825 1.00118.26 C ANISOU 2434 CD GLU A 311 16690 18962 9279 2336 633 -2227 C ATOM 2435 OE1 GLU A 311 -21.868 16.006 -28.836 1.00120.23 O ANISOU 2435 OE1 GLU A 311 16851 19448 9384 2295 676 -2107 O ATOM 2436 OE2 GLU A 311 -23.611 15.118 -27.777 1.00118.78 O1- ANISOU 2436 OE2 GLU A 311 16969 18824 9339 2264 523 -2436 O1- ATOM 2437 N ARG A 312 -19.480 15.955 -24.088 1.00111.76 N ANISOU 2437 N ARG A 312 15222 18119 9122 2693 934 -1773 N ATOM 2438 CA ARG A 312 -18.272 16.760 -23.883 1.00112.99 C ANISOU 2438 CA ARG A 312 15100 18511 9320 2765 1081 -1615 C ATOM 2439 C ARG A 312 -17.430 16.271 -22.690 1.00116.02 C ANISOU 2439 C ARG A 312 15395 18782 9903 2941 1112 -1640 C ATOM 2440 O ARG A 312 -16.205 16.305 -22.782 1.00116.56 O ANISOU 2440 O ARG A 312 15278 19059 9952 3109 1261 -1628 O ATOM 2441 CB ARG A 312 -18.651 18.252 -23.752 1.00112.28 C ANISOU 2441 CB ARG A 312 14827 18515 9320 2525 1040 -1353 C ATOM 2442 CG ARG A 312 -17.465 19.234 -23.802 1.00114.04 C ANISOU 2442 CG ARG A 312 14763 18979 9588 2541 1199 -1189 C ATOM 2443 CD ARG A 312 -16.947 19.454 -25.234 1.00119.15 C ANISOU 2443 CD ARG A 312 15362 19932 9979 2527 1351 -1130 C ATOM 2444 NE ARG A 312 -15.702 20.232 -25.266 1.00122.39 N ANISOU 2444 NE ARG A 312 15502 20586 10413 2567 1542 -1029 N ATOM 2445 CZ ARG A 312 -15.158 20.793 -26.361 1.00125.83 C ANISOU 2445 CZ ARG A 312 15838 21293 10678 2503 1704 -912 C ATOM 2446 NH1 ARG A 312 -14.008 21.469 -26.251 1.00127.28 N1+ ANISOU 2446 NH1 ARG A 312 15761 21675 10925 2507 1876 -833 N1+ ATOM 2447 NH2 ARG A 312 -15.743 20.687 -27.563 1.00127.26 N1+ ANISOU 2447 NH2 ARG A 312 16176 21486 10692 2397 1670 -860 N1+ ATOM 2448 N LEU A 313 -18.103 15.785 -21.630 1.00118.07 N ANISOU 2448 N LEU A 313 15783 18730 10347 2908 975 -1675 N ATOM 2449 CA LEU A 313 -17.514 15.131 -20.458 1.00119.14 C ANISOU 2449 CA LEU A 313 15876 18741 10652 3097 987 -1700 C ATOM 2450 C LEU A 313 -16.778 13.823 -20.814 1.00125.22 C ANISOU 2450 C LEU A 313 16796 19486 11294 3414 1090 -1916 C ATOM 2451 O LEU A 313 -15.681 13.596 -20.304 1.00126.78 O ANISOU 2451 O LEU A 313 16850 19787 11534 3653 1181 -1922 O ATOM 2452 CB LEU A 313 -18.639 14.912 -19.415 1.00115.82 C ANISOU 2452 CB LEU A 313 15593 17981 10433 2973 824 -1679 C ATOM 2453 CG LEU A 313 -18.263 14.145 -18.125 1.00114.97 C ANISOU 2453 CG LEU A 313 15545 17668 10470 3182 813 -1730 C ATOM 2454 CD1 LEU A 313 -17.129 14.824 -17.340 1.00113.97 C ANISOU 2454 CD1 LEU A 313 15115 17683 10505 3198 822 -1556 C ATOM 2455 CD2 LEU A 313 -19.503 13.925 -17.234 1.00113.26 C ANISOU 2455 CD2 LEU A 313 15603 17071 10360 3072 681 -1790 C ATOM 2456 N ILE A 314 -17.386 13.002 -21.689 1.00129.81 N ANISOU 2456 N ILE A 314 17667 19939 11717 3427 1075 -2103 N ATOM 2457 CA ILE A 314 -16.824 11.736 -22.170 1.00135.21 C ANISOU 2457 CA ILE A 314 18550 20540 12284 3731 1172 -2327 C ATOM 2458 C ILE A 314 -15.596 11.948 -23.079 1.00140.19 C ANISOU 2458 C ILE A 314 18979 21499 12789 3908 1346 -2328 C ATOM 2459 O ILE A 314 -14.610 11.228 -22.925 1.00142.07 O ANISOU 2459 O ILE A 314 19172 21735 13073 4182 1431 -2386 O ATOM 2460 CB ILE A 314 -17.901 10.880 -22.910 1.00136.80 C ANISOU 2460 CB ILE A 314 19115 20514 12351 3649 1111 -2537 C ATOM 2461 CG1 ILE A 314 -18.988 10.403 -21.918 1.00134.53 C ANISOU 2461 CG1 ILE A 314 19006 19860 12249 3449 945 -2528 C ATOM 2462 CG2 ILE A 314 -17.356 9.668 -23.705 1.00140.68 C ANISOU 2462 CG2 ILE A 314 19800 20865 12787 3897 1210 -2733 C ATOM 2463 CD1 ILE A 314 -20.288 9.934 -22.590 1.00135.66 C ANISOU 2463 CD1 ILE A 314 19487 19779 12278 3319 879 -2745 C ATOM 2464 N HIS A 315 -15.670 12.941 -23.983 1.00141.94 N ANISOU 2464 N HIS A 315 19064 21981 12884 3734 1392 -2239 N ATOM 2465 CA HIS A 315 -14.605 13.277 -24.933 1.00147.66 C ANISOU 2465 CA HIS A 315 19594 22993 13518 3843 1560 -2218 C ATOM 2466 C HIS A 315 -13.402 13.992 -24.291 1.00149.29 C ANISOU 2466 C HIS A 315 19439 23438 13846 3926 1647 -2068 C ATOM 2467 O HIS A 315 -12.292 13.844 -24.801 1.00153.20 O ANISOU 2467 O HIS A 315 19766 24133 14312 4089 1787 -2087 O ATOM 2468 CB HIS A 315 -15.176 14.117 -26.096 1.00149.34 C ANISOU 2468 CB HIS A 315 19790 23398 13554 3623 1587 -2150 C ATOM 2469 CG HIS A 315 -16.284 13.479 -26.905 1.00152.99 C ANISOU 2469 CG HIS A 315 20566 23703 13862 3572 1529 -2329 C ATOM 2470 CD2 HIS A 315 -17.284 14.042 -27.669 1.00154.24 C ANISOU 2470 CD2 HIS A 315 20801 23971 13832 3412 1523 -2331 C ATOM 2471 ND1 HIS A 315 -16.495 12.111 -26.977 1.00153.92 N ANISOU 2471 ND1 HIS A 315 20968 23509 14007 3683 1469 -2540 N ATOM 2472 CE1 HIS A 315 -17.569 11.914 -27.745 1.00155.77 C ANISOU 2472 CE1 HIS A 315 21428 23678 14081 3575 1429 -2679 C ATOM 2473 NE2 HIS A 315 -18.100 13.041 -28.201 1.00155.66 N ANISOU 2473 NE2 HIS A 315 21288 23928 13929 3419 1453 -2556 N ATOM 2474 N SER A 316 -13.627 14.738 -23.194 1.00146.45 N ANISOU 2474 N SER A 316 18952 23073 13621 3809 1568 -1928 N ATOM 2475 CA SER A 316 -12.576 15.431 -22.443 1.00146.73 C ANISOU 2475 CA SER A 316 18635 23338 13778 3863 1642 -1802 C ATOM 2476 C SER A 316 -11.744 14.505 -21.537 1.00148.21 C ANISOU 2476 C SER A 316 18802 23438 14075 4183 1644 -1904 C ATOM 2477 O SER A 316 -10.613 14.871 -21.218 1.00148.26 O ANISOU 2477 O SER A 316 18525 23683 14123 4323 1743 -1877 O ATOM 2478 CB SER A 316 -13.185 16.621 -21.672 1.00142.92 C ANISOU 2478 CB SER A 316 18032 22791 13481 3578 1524 -1599 C ATOM 2479 OG SER A 316 -14.018 16.226 -20.600 1.00141.87 O ANISOU 2479 OG SER A 316 18124 22287 13492 3532 1342 -1625 O ATOM 2480 N LEU A 317 -12.298 13.342 -21.150 1.00148.94 N ANISOU 2480 N LEU A 317 19191 23187 14213 4298 1532 -2016 N ATOM 2481 CA LEU A 317 -11.625 12.337 -20.327 1.00152.46 C ANISOU 2481 CA LEU A 317 19680 23501 14749 4627 1526 -2104 C ATOM 2482 C LEU A 317 -10.992 11.293 -21.279 1.00158.84 C ANISOU 2482 C LEU A 317 20617 24286 15448 4845 1623 -2259 C ATOM 2483 O LEU A 317 -11.743 10.589 -21.957 1.00163.79 O ANISOU 2483 O LEU A 317 21529 24744 15960 4768 1619 -2374 O ATOM 2484 CB LEU A 317 -12.678 11.707 -19.377 1.00148.70 C ANISOU 2484 CB LEU A 317 19511 22622 14367 4644 1382 -2149 C ATOM 2485 CG LEU A 317 -12.136 11.259 -17.996 1.00145.65 C ANISOU 2485 CG LEU A 317 19126 22097 14119 4924 1335 -2148 C ATOM 2486 CD1 LEU A 317 -11.061 10.150 -18.053 1.00147.58 C ANISOU 2486 CD1 LEU A 317 19547 22204 14322 5266 1393 -2291 C ATOM 2487 CD2 LEU A 317 -11.706 12.460 -17.126 1.00143.64 C ANISOU 2487 CD2 LEU A 317 18433 22167 13976 4932 1345 -1994 C ATOM 2488 N PRO A 318 -9.641 11.216 -21.351 1.00157.97 N ANISOU 2488 N PRO A 318 20302 24353 15367 5112 1707 -2274 N ATOM 2489 CA PRO A 318 -8.955 10.318 -22.299 1.00162.89 C ANISOU 2489 CA PRO A 318 21024 24992 15876 5318 1816 -2415 C ATOM 2490 C PRO A 318 -9.112 8.828 -21.939 1.00168.81 C ANISOU 2490 C PRO A 318 22114 25373 16652 5598 1772 -2560 C ATOM 2491 O PRO A 318 -8.869 8.450 -20.793 1.00168.28 O ANISOU 2491 O PRO A 318 22060 25171 16709 5789 1697 -2529 O ATOM 2492 CB PRO A 318 -7.489 10.780 -22.237 1.00163.42 C ANISOU 2492 CB PRO A 318 20667 25458 15968 5454 1924 -2346 C ATOM 2493 CG PRO A 318 -7.321 11.345 -20.837 1.00159.70 C ANISOU 2493 CG PRO A 318 19944 25074 15661 5429 1835 -2208 C ATOM 2494 CD PRO A 318 -8.676 11.983 -20.557 1.00155.50 C ANISOU 2494 CD PRO A 318 19647 24249 15187 5237 1699 -2168 C ATOM 2495 N THR A 319 -9.525 8.030 -22.941 1.00172.83 N ANISOU 2495 N THR A 319 22914 25717 17035 5616 1822 -2718 N ATOM 2496 CA THR A 319 -9.694 6.569 -22.905 1.00180.13 C ANISOU 2496 CA THR A 319 24195 26285 17960 5865 1817 -2876 C ATOM 2497 C THR A 319 -10.756 6.053 -21.897 1.00182.42 C ANISOU 2497 C THR A 319 24750 26181 18380 5856 1679 -2861 C ATOM 2498 O THR A 319 -10.714 4.883 -21.510 1.00188.28 O ANISOU 2498 O THR A 319 25509 26801 19228 6113 1643 -2825 O ATOM 2499 CB THR A 319 -8.346 5.789 -22.752 1.00184.47 C ANISOU 2499 CB THR A 319 24585 26984 18520 6245 1907 -2899 C ATOM 2500 CG2 THR A 319 -7.197 6.332 -23.618 1.00186.40 C ANISOU 2500 CG2 THR A 319 24555 27630 18639 6234 2056 -2910 C ATOM 2501 OG1 THR A 319 -7.901 5.634 -21.416 1.00184.14 O ANISOU 2501 OG1 THR A 319 24279 27066 18619 6378 1841 -2756 O ATOM 2502 N SER A 320 -11.712 6.921 -21.519 1.00181.07 N ANISOU 2502 N SER A 320 24789 25820 18188 5546 1601 -2886 N ATOM 2503 CA SER A 320 -12.844 6.594 -20.651 1.00180.64 C ANISOU 2503 CA SER A 320 25000 25389 18245 5468 1478 -2878 C ATOM 2504 C SER A 320 -13.868 5.692 -21.366 1.00181.86 C ANISOU 2504 C SER A 320 25576 25193 18329 5289 1454 -3056 C ATOM 2505 O SER A 320 -14.111 5.877 -22.560 1.00183.72 O ANISOU 2505 O SER A 320 25846 25536 18422 5142 1499 -3156 O ATOM 2506 CB SER A 320 -13.489 7.912 -20.179 1.00174.26 C ANISOU 2506 CB SER A 320 23984 24715 17511 5218 1383 -2714 C ATOM 2507 OG SER A 320 -14.522 7.693 -19.239 1.00171.85 O ANISOU 2507 OG SER A 320 23954 24040 17303 5127 1272 -2716 O ATOM 2508 N LEU A 321 -14.465 4.757 -20.607 1.00174.94 N ANISOU 2508 N LEU A 321 25021 23897 17550 5293 1383 -3095 N ATOM 2509 CA LEU A 321 -15.543 3.880 -21.067 1.00170.49 C ANISOU 2509 CA LEU A 321 24858 22979 16943 5082 1354 -3269 C ATOM 2510 C LEU A 321 -16.844 4.673 -21.292 1.00162.46 C ANISOU 2510 C LEU A 321 23792 22053 15882 4679 1257 -3251 C ATOM 2511 O LEU A 321 -17.187 5.538 -20.484 1.00159.78 O ANISOU 2511 O LEU A 321 23226 21877 15607 4566 1185 -3087 O ATOM 2512 CB LEU A 321 -15.717 2.731 -20.044 1.00170.40 C ANISOU 2512 CB LEU A 321 25199 22486 17060 5169 1317 -3295 C ATOM 2513 CG LEU A 321 -16.783 1.662 -20.395 1.00 0.00 C ATOM 2514 CD1 LEU A 321 -16.511 0.974 -21.751 1.00 0.00 C ATOM 2515 CD2 LEU A 321 -16.938 0.643 -19.245 1.00 0.00 C ATOM 2516 N GLU A 322 -17.540 4.347 -22.393 1.00159.99 N ANISOU 2516 N GLU A 322 23688 21648 15453 4463 1251 -3424 N ATOM 2517 CA GLU A 322 -18.719 5.045 -22.918 1.00155.08 C ANISOU 2517 CA GLU A 322 23016 21145 14761 4091 1147 -3420 C ATOM 2518 C GLU A 322 -19.923 4.551 -22.134 1.00154.86 C ANISOU 2518 C GLU A 322 23307 20726 14808 3845 1043 -3518 C ATOM 2519 O GLU A 322 -21.071 4.919 -22.381 1.00155.30 O ANISOU 2519 O GLU A 322 23501 20736 14768 3571 986 -3662 O ATOM 2520 CB GLU A 322 -18.892 4.777 -24.441 1.00155.62 C ANISOU 2520 CB GLU A 322 23061 21439 14629 3986 1191 -3539 C ATOM 2521 CG GLU A 322 -17.715 5.198 -25.358 1.00153.92 C ANISOU 2521 CG GLU A 322 22588 21563 14330 4232 1327 -3479 C ATOM 2522 CD GLU A 322 -16.466 4.305 -25.316 1.00154.36 C ANISOU 2522 CD GLU A 322 22826 21449 14377 4535 1451 -3625 C ATOM 2523 OE1 GLU A 322 -16.579 3.149 -24.848 1.00154.74 O ANISOU 2523 OE1 GLU A 322 23232 21125 14438 4504 1441 -3805 O ATOM 2524 OE2 GLU A 322 -15.411 4.800 -25.765 1.00154.37 O1- ANISOU 2524 OE2 GLU A 322 22607 21688 14359 4796 1561 -3561 O1- TER HETATM 2525 C1 UNK Z 999 -29.892 29.867 7.317 1.00 0.00 C HETATM 2526 N1 UNK Z 999 -29.285 29.242 6.294 1.00 0.00 N HETATM 2527 O1 UNK Z 999 -30.885 29.443 7.907 1.00 0.00 O HETATM 2528 S1 UNK Z 999 -31.804 28.280 3.031 1.00 0.00 S HETATM 2529 C2 UNK Z 999 -29.687 27.940 5.757 1.00 0.00 C HETATM 2530 N2 UNK Z 999 -27.946 26.732 7.086 1.00 0.00 N HETATM 2531 O2 UNK Z 999 -30.083 25.928 6.918 1.00 0.00 O HETATM 2532 C3 UNK Z 999 -29.223 26.756 6.629 1.00 0.00 C HETATM 2533 N3 UNK Z 999 -27.047 25.949 10.603 1.00 0.00 N HETATM 2534 O3 UNK Z 999 -28.689 27.133 9.665 1.00 0.00 O HETATM 2535 C4 UNK Z 999 -29.289 27.811 4.271 1.00 0.00 C HETATM 2536 N4 UNK Z 999 -29.184 25.002 13.535 1.00 0.00 N HETATM 2537 O4 UNK Z 999 -29.304 24.529 11.316 1.00 0.00 O HETATM 2538 C5 UNK Z 999 -30.081 28.757 3.349 1.00 0.00 C HETATM 2539 N5 UNK Z 999 -26.885 19.533 13.318 1.00 0.00 N1+ HETATM 2540 O5 UNK Z 999 -31.884 25.699 12.919 1.00 0.00 O1- HETATM 2541 C6 UNK Z 999 -31.564 27.141 1.641 1.00 0.00 C HETATM 2542 O6 UNK Z 999 -32.516 23.562 13.253 1.00 0.00 O HETATM 2543 C7 UNK Z 999 -27.354 25.860 8.140 1.00 0.00 C HETATM 2544 C8 UNK Z 999 -27.732 26.384 9.540 1.00 0.00 C HETATM 2545 C9 UNK Z 999 -27.764 24.357 8.003 1.00 0.00 C HETATM 2546 C10 UNK Z 999 -26.933 23.326 8.836 1.00 0.00 C HETATM 2547 C11 UNK Z 999 -27.789 22.129 9.322 1.00 0.00 C HETATM 2548 C12 UNK Z 999 -25.646 22.897 8.106 1.00 0.00 C HETATM 2549 C13 UNK Z 999 -27.545 26.016 11.986 1.00 0.00 C HETATM 2550 C14 UNK Z 999 -28.754 25.094 12.261 1.00 0.00 C HETATM 2551 C15 UNK Z 999 -26.348 25.865 12.954 1.00 0.00 C HETATM 2552 C16 UNK Z 999 -25.771 27.225 13.286 1.00 0.00 C HETATM 2553 C17 UNK Z 999 -26.028 27.812 14.541 1.00 0.00 C HETATM 2554 C18 UNK Z 999 -25.685 29.138 14.762 1.00 0.00 C HETATM 2555 C19 UNK Z 999 -25.134 29.900 13.740 1.00 0.00 C HETATM 2556 C20 UNK Z 999 -24.885 29.335 12.498 1.00 0.00 C HETATM 2557 C21 UNK Z 999 -25.180 28.001 12.268 1.00 0.00 C HETATM 2558 C22 UNK Z 999 -30.352 24.249 14.051 1.00 0.00 C HETATM 2559 C23 UNK Z 999 -31.720 24.523 13.318 1.00 0.00 C HETATM 2560 C24 UNK Z 999 -30.025 22.741 14.296 1.00 0.00 C HETATM 2561 C25 UNK Z 999 -29.900 21.841 13.043 1.00 0.00 C HETATM 2562 C26 UNK Z 999 -29.151 20.521 13.259 1.00 0.00 C HETATM 2563 C27 UNK Z 999 -27.683 20.715 13.669 1.00 0.00 C CONECT 2525 2526 2527 CONECT 2526 2525 2529 CONECT 2527 2525 CONECT 2528 2541 2538 CONECT 2529 2526 2532 2535 CONECT 2530 2543 2532 CONECT 2531 2532 CONECT 2532 2529 2530 2531 CONECT 2533 2549 2544 CONECT 2534 2544 CONECT 2535 2529 2538 CONECT 2536 2558 2550 CONECT 2537 2550 CONECT 2538 2535 2528 CONECT 2539 2563 CONECT 2540 2559 CONECT 2541 2528 CONECT 2542 2559 CONECT 2543 2530 2544 2545 CONECT 2544 2543 2533 2534 CONECT 2545 2543 2546 CONECT 2546 2545 2547 2548 CONECT 2547 2546 CONECT 2548 2546 CONECT 2549 2533 2550 2551 CONECT 2550 2549 2536 2537 CONECT 2551 2549 2552 CONECT 2552 2551 2553 2557 CONECT 2553 2552 2554 CONECT 2554 2553 2555 CONECT 2555 2554 2556 CONECT 2556 2555 2557 CONECT 2557 2552 2556 CONECT 2558 2536 2559 2560 CONECT 2559 2558 2540 2542 CONECT 2560 2558 2561 CONECT 2561 2560 2562 CONECT 2562 2561 2563 CONECT 2563 2562 2539 END